Immunonephelometric and Immunoturbidimetric Assays for Proteins

References

• Libby R. L. The photonreflectometer - an instrument for the measurement of turbid systems. J. Immunol. 1938; 34: 71
   Google Scholar
• Libby R. L. A new and rapid quantitation technique for the determination of the potency of Type I and Type II anti-pneumococcal serum. J. Immunol. 1938; 34: 269
   Google Scholar
• Chow B. F. The determination of plasma or serum albumin by means of a precipitin reaction. J. Biol. Chem. 1947; 167: 757
   PubMedGoogle Scholar
• Gitlin G., Edelhoch H. A study of the reaction between human serum albumin and its homologous equine antibody through the measurement of light scattering. J. Immunol. 1951; 66: 67
   PubMed Web of Science ®Google Scholar
• Schultze J. E., Schwick G. Quantitative Immunologische bestimmung von plasmaproteinen. Clin. Chim. Acta. 1959; 4: 15
   PubMed Web of Science ®Google Scholar
• Ritchie R. F., Alper C. A., Graves J. A. Experience with a fully automated system for immunoassay of specific serum proteins. Arthritis Rheum. 1969; 12: 693
   Google Scholar
• Savory J., Buffone G. J., Reich R. Kinetics of the IgG anti-IgG reaction as evaluated by conventional and stopped flow nephelometry. Clin. Chem. 1974; 20: 1071
   PubMed Web of Science ®Google Scholar
• Tyndall J. On some phenomena connected with the motion of liquids. Proc. R. Inst. 1854; 1: 446
   Google Scholar
• Rayleigh Lord. On the scattering of light by small particles. Phil. 1871; 41: 447, Mag.
   Google Scholar
• Rayleigh Lord. On the light from the sky, its polarisation and colour. Phil. Mag. 1871; 41: 107
   Google Scholar
• Tanford C. Light scattering. Physical Chemistry of Macromolecules. John Wiley Sons, New York 1961; 275
   Google Scholar
• Van Holde K. E. Scattering in Physical Biochemistry. Prentice-Hall, Englewood Cliffs, NJ 1971; Vol. 9
   Google Scholar
• Karker M. The Scattering of Light and Other Electromagnetic Radiation. Academic Press, New York 1969
   Google Scholar
• Rayleigh Lord. On the electromagnetic theory of light. Phil. Mag. 1881; 12: 81
   Google Scholar
• Rayleigh Lord. The incidence of light upon a transparent sphere of dimensions comparable with wavelength. Proc. R. Soc. 1910; A84: 25
   Google Scholar
• Debye P. Zerstreung Von Rontgerstrahen. Ann. Physik 1915; 46: 809
   Google Scholar
• Mie G. Ann. Physik. 1908; 25: 377
   Google Scholar
• Kusnetz J., Mansberg H. P. Optical considerations: nephelometry. Automated Immuno-analysis. Part I, R. F. Ritchie. Marcel Dekker, New York 1978; 1
   Google Scholar
• Steward M. W. Affinity of the antibody-antigen reaction and its biological significance. Structure and Function of Antibodies, L. E. Glyn, M. W. Steward. John Wiley & Sons, New York 1977; 233
   Google Scholar
• Buffone G. J., Savory J., Hermans J. Evaluation of kinetic light scattering as an approach for the measurement of specific proteins using the centrifugal fast analyser. II. Theoretical considerations. Clin. Chem. 1975; 21: 1735
   PubMed Web of Science ®Google Scholar
• Anderson R. J., Sternberg J. C. A rate nepheiometer for immunoprecipitin measurement of serum proteins. Automated Immunoanalysis Part 2, R. F. Ritchie. Marcel Dekker, New York 1978; 409
   Google Scholar
• Whicher J., Blow C. Formulation of optimal conditions for an immunonephelometric assay. Ann. Clin. Biochem. 1980; 7: 170
   Google Scholar
• Sternberg J. C. A rate nepheiometer for measuring specific proteins by immunoprecipitin reactions. Clin. Chem. 1977; 23: 1456
   PubMed Web of Science ®Google Scholar
• Cambiaso C. L., Masson P. L., Vaerman J. P., Heremans J. F. Automated nephelometric immunoassay (ANIA) I. Importance of antibody affinity. J. Immunol. Methods 1974; 5: 153
   PubMedGoogle Scholar
• Anthony F., Spencer K., Mason P., Massom G. M., Price C. P., Wood P. J. The variable influence of an a-component in pregnancy plasma on four different assay systems for the measurement of pregnancy specific/3i-glycoprotein. Clin. Chim. Acta 1980; 105: 287
   PubMedGoogle Scholar
• Ritchie R. F. Evaluation of antibody preparations for the AIP system, Colloq., AIP, Brussels. 1972; 59
   Google Scholar
• Marrack J. R., Richards C. B. Light scattering studies of the formation and aggregates in mixtures of antigen and antibody. Immunology 1971; 20: 1019
   PubMed Web of Science ®Google Scholar
• Dandliker W. B., Alonso R., de Saussere V. A., Kierzenbaum F., Levison S. A., Schapiro H.C. The effect of chaotropic ions on the dissociation of antigen-antibody complexes. Biochemistry 1967; 6: 1460
   PubMed Web of Science ®Google Scholar
• Killingsworth L. M., Savory J. Nephelometric studies of the precipitin reaction: a model system for specific protein measurements. Clin. Chem. 1973; 19: 403
   PubMedGoogle Scholar
• Price C. P., Spencer K. Kinetic immunoturbidimetry of human choriomammotrophin in serum. Clin. Chem. 1981; 27: 882
   PubMedGoogle Scholar
• Marrack J. R., Grant R. A. The interaction of antigen and antibody in low concentrations of salt. Br. J. Exp. Pathol. 1953; 34: 263
   PubMedGoogle Scholar
• Hellsing K., Laurent T. C. The influence of dextran on the precipitin reaction. Acta Chem. Scand. 1964; 18: 1303
   Google Scholar
• Ceska M. Antigen-antibody interation in the presence of water soluble non-ionic resins. Biochim. Biophys. Acta. 1969; 177: 625
   PubMedGoogle Scholar
• Adams L. S., Terry L. M. Detection of human IgA subclones and allotypes by polymer-induced precipitation in agarose gel. J. Immunol. Methods 1974; 6: 157
   PubMedGoogle Scholar
• Kostner G., Holasek J. Influence of dextrans and polyethylene glycol on sensitivity of two-dimensional immunoelectrophoresis and electroimmunodiffusion. Anal. Biochem. 1972; 46: 680
   PubMedGoogle Scholar
• Lundkvist V., Ceska M. Effect of non-ionic polymers on the formation of immunoprecipitates in single radial immunodiffusion techniques. Immunology 1972; 23: 413
   PubMedGoogle Scholar
• Hellsing K. Enhancing effects of non-ionic polymers on immunochemical reactions. Automated Immunoanalysis Part I, R. F. Ritchie. Marcel Dekker, New York 1978; 67
   Google Scholar
• Laurent T. C., Killander J. A theory of gel filtration and its experimental verification. J. Chromatogr. 1964; 14: 317
   Web of Science ®Google Scholar
• Hellsing K. The effects of different polymers for the enhancement of the antibody-antigen reaction as measured with nephelometry. Protides of the Biological Fluids, H. Peters. Pergamon Press, Oxford 1974; Vol. 21.: 579
   Google Scholar
• Price C. P., Spencer K. Unpublished observations
   Google Scholar
• Buffone G. J., Savory J., Hermans J. Evaluation of kinetic light scattering as an approach to the measurement of proteins with the centrifugal fast analyser. II. Theoretical considerations. Clin. Chem. 1975; 21: 1735
   PubMed Web of Science ®Google Scholar
• Ritchie R. F. Automated immunoprecipitation analysis of serum proteins. The Plasma Proteins, F. W. Putnam. Academic Press, New York 1975; Vol. 2: 375
   Google Scholar
• Laurel C.-B. Electroimmunoassay. Scand. J. Clin. Lab. Invest. 1972; 29((Suppl. 124))21
   Google Scholar
• Deverill I. Kinetic measurements pf the immunoprecipitin reaction using the centrifugal analyser. Centrifugal Analyses in Clinical Chemistry, C. P. Price, K. Spencer. Praeger, New York 1980; 109
   Google Scholar
• Whicher J. T., Perry D. E., Hobbs J. R. An evaluation of the Hyland laser nephelometer PDQ systems for the measurement of immunoglobulins. Ann. Clin. Biochem. 1978; 15: 77
   PubMed Web of Science ®Google Scholar
• Spencer K., Price C. P. Clinical chemistry instrumentation and light scattering measurement. U. V. Spectro. Group Bull. 1981; 8: 38
   Google Scholar
• Hellsing K., Enstrom H. Pre-treatment of serum samples for immunonephelometric analysis by precipitation by polyethylene glycol. Scand. J. Clin. Lab. Invest. 1977; 37: 529
   PubMed Web of Science ®Google Scholar
• Wood J. P., Cockett D., Mason P. A rapid and inexpensive laser nephelometric assay for plasma pregnancy specific /3i-glycoprotein levels. Clin. Chim. Acta 1978; 90: 87
   PubMedGoogle Scholar
• Kallner A. Removal of background interference in nephelometric determination of serum proteins. Clin. Chim. Acta. 1977; 80: 293
   PubMedGoogle Scholar
• Walsh R. L., Coles M. E. Binding of IgG and other proteins to microfilters. Clin. Chem. 1980; 26: 496
   PubMed Web of Science ®Google Scholar
• Pardue H. L. A comprehensive classification of kinetic methods of analysis used in clinical chemistry. Clin. Chem. 1977; 23: 2189
   PubMedGoogle Scholar
• Muller-Mathesius R., Opper C. Influence of measurement time and reaction medium on kinetic immunoturbidimetric protein determination. J. Clin. Chem. Clin. Biochem. 1980; 18: 501
   PubMedGoogle Scholar
• Whicher J. T. Problems encountered in immunochemical technique: Methodology. Immuno-chemistry in Clinical Laboratory Medicine, A. Milford-Ward, J. T. Whicher. MTP Press, LancasterEngland 1979; 51
   Google Scholar
• Franklin E. C., Buxbaum J. Immunoglobulins in the normal state and in neoplasms of B cells. Comprehensive Immunology, R. A. Good, S. B. Day. Plenum Press, New York 1978; Vol. 4: 361
   Google Scholar
• Renoe B. W., Savory J., Buffone G. J., Cross R. E. Laser nephelometry and the measurement of specific proteins. Centrifugal Analysers in Clinical Chemistry, C. P. Price, K. Spencer. Praeger, EastbourneEngland 1980; 395
   Google Scholar
• Spencer K., Price C. P. Kinetic immunoturbidimetry: the estimation of albumin. Clin. Chim. Acta 1979; 95: 263
   PubMed Web of Science ®Google Scholar
• Hills L. P., Tiffany T. O. Comparison of turbidimetric and light scattering measurements of immunoglobulins by use of a centrifugal analyser with absorbance/ fluorescence light scattering optics. Clin. Chem. 1980; 26: 1459
   PubMed Web of Science ®Google Scholar
• Spencer K., Price C. P., Anthony F., Wood P. J. Kinetic immunoturbidimetry: the measurement of pregnancy specific/3i-glycoprotein. Clin. Chim. Acta 1979; 99: 177
   PubMedGoogle Scholar
• Killingsworth L. M., Savory J. Manual nephelometric methods for immunochemical determination of immunoglobulins IgG, IgA, and lgM, in human serum. Clin. Chem. 1972; 18: 335
   PubMed Web of Science ®Google Scholar
• Deaton C. O., Maxwell K. W., Smith R. S., Creveling R. L. Use of laser nephelometry in the measurement of serum proteins. Clin. Chem. 1976; 22: 1
   Google Scholar
• Alper C. A., Propp R. P. Genetic polymorphism of the third component of human complement (C3). J. Clin. Invest. 1968; 47: 2181
   PubMed Web of Science ®Google Scholar
• Ritchie R. F., Alper C. A., Graves J. A. Experience with a full automated system for immunoassay of specific serum proteins. Arthritis Rheum. 1969; 12: 693
   Google Scholar
• Alper C. A., Abramson N., Johnston R. B., Janek J. H., Rosen F. B. Studies in vivo and in vitro on an abnormality in the metabolism of C3 in a patient with increased susceptibility to infection. J. Clin. Invest. 1970; 18(3)49–257, 1975
   Google Scholar
• Eckman I., Robbins J. B., Van der Hammer C. J., Lentz J., Scheinberg H. I. Automation of quantitative microanalysis of human serum transferrin: a model system. Clin. Chem. 1970; 16: 558
   PubMed Web of Science ®Google Scholar
• Ritchie R. F., Graves J. A. Automated analysis of cerebrospinal fluid proteins. Technicon Int. Cong. Advances in Automated Analysis. Technicon Instrument Corp., Tarrytown, NY 1970; Vol. 1: 117
   Google Scholar
• Killingsworth L. M., Savory J. Automated immunochemical procedure for the measurement of immunoglobulin IgG, IgA, and IgM in human serum. Clin. Chem. 1971; 17: 936
   PubMed Web of Science ®Google Scholar
• Killingsworth L. M., Savory J., Teague P. O. Automated immunoprecipitation technique for the analysis of the third component of complement in human serum. Clin. Chem. 1971; 17: 374
   PubMed Web of Science ®Google Scholar
• Larson C, Orenstein P., Ritchie R. F. An automated method for the quantitation of proteins in body fluids, Technicon Int. Cong. Advances in Automated Analysis. Technicon Instrument Corp., Tarrytown, NY 1971; Vol. I: 104
   Google Scholar
• Aitken J. Automated analysis of a,-antitrypsin and immunoglobulins, Colloq. Univ. Louvain, Belgium. Technicon Alp Monograph. 33 Technicon Instrument Corp., Tarrytown, NY 1973, 1972
   Google Scholar
• Halberstam D., Diamond H. S., Derrico E. Analysis of serum a,-antitrypsin, Technicon Int. Cong. Advances in Automated Analysis. Technicon Instrument Corp., Tarrytown, NY 1972; Vol 4: 23
   Google Scholar
• Markowitz H., Tschida A. R. Automated quantitative immunochemica analysis of human immunoglobulins. Clin. Chem. 1972; 18: 1364
   PubMed Web of Science ®Google Scholar
• Ritchie R. F., Clark C. Fully automated analysis of low density lipoproteins. Colloq. Univ. Louvain, Belgium. Technicon A IP Monograph 33. Technicon Instrument Corp., Tarrytown, NY 1973, 1972
   Google Scholar
• Killingsworth L. M., Savory J. Manual nephelometric methods for the determination of IgG, IgA and in human serum. Clin. Chem. 1972; 18: 335
   PubMed Web of Science ®Google Scholar
• Savory J., Heintges M. G., Killingsworth L. M., Potter J. M. Manual and automated determination of immunoglobulins in unconcentrated cerebrospinal fluid. Clin. Chem. 1972; 18: 37
   PubMed Web of Science ®Google Scholar
• Durrington P. N., Whicher J. T., Warren C, Bolton C. H., Hartog M. A comparison of methods for the immunoassay of apolipoprotein B in man. C 7. Chim. Acta 1976; 71: 95
   PubMedGoogle Scholar
• Tiffany T. O., Parella J. M., Johnson W. F., Burton C. A. Specific protein analysis by light scatter measurement with a miniature centrifugal analyser. Clin. Chem. 1974; 20: 1055
   PubMed Web of Science ®Google Scholar
• Hellsing K. Influence of polymers on the antigen-antibody reaction in a continuous flow system. Colloq. Univ. Louvain, Belgium. Technicon AlP Monograph 17. Technicon Instrument Corp., Tarrytown, NY 1973, 1972
   Google Scholar
• Marcroft J., Newbanks I. M. Evaluation of a specific protein analyser. Clin. Chim. Acta 1973; 46: 399
   PubMed Web of Science ®Google Scholar
• Tiffany T. O. The concepts of centrifugal analysers. Centrifugal Analysers in Clinical Chemistry, C. P. Price, K. Spencer. Praeger, New York 1980; 109
   Google Scholar
• Munley J., Swanson J. R., Morris R. L. Laser modification of a Union Carbide Centrifichem Model 300 for use in kinetic and equilibrium determination of body fluid proteins. Clin. Chem. 1976; 22: 1196
   Google Scholar
• Kenny T., Swanson J. R. Comparison of turbidimetric and nephelometric methods for measuring IgG in human serum using a Centrifichem 300. Clin. Chem. 1977; 23: 1160
   Google Scholar
• Stone M. C., Thorpe J. M. A new technique for the investigation of the low-density lipoproteins in health and disease. Clin. Chim. Ada 1966; 14: 812
   Web of Science ®Google Scholar
• Thorpe J. M., Horsfall G. B., Stone M.C. A new red sensitive micronephelometer. Med. Biol. Eng. 1967; 5: 51
   PubMedGoogle Scholar
• Whicher J. T., Hunt J., Dando T., Perry D. E. An Evaluation of the Kallestad Nephelometer for the Measurement of Proteins, Sci. Tech. Branch. Department of Health and Social Security. London 1979
   Google Scholar
• Sieber A., Gross J. Determination of serum proteins by laser nephelometry. Protides Biol. Fluids 1976; 23: 295
   Google Scholar
• Skelton M. J., Hosking C. S. An evaluation of the Hyland laser nephelometer PDQ. Aust. J. Med. Technoi 1977; 8: 33
   Google Scholar
• Walsh R. L., Coles M. E., Geary T. D. Evaluation of two commercially available nephelometers and their recommended methods for measurement of immunoglobulin G. Clin. Chem. 1976; 25: 151
   Google Scholar
• Blow C. Unpublished observations
   Google Scholar
• Van Lenti F., Marchand A., Galen R. S. Evaluation of a nephelometric assay for haptoglobin and its clinical usefulness. Clin. Chem. 1979; 25: 2007
   PubMedGoogle Scholar
• Buffone G. J., Savory J., Cross R. E. Use of a laser modified centrifugal analyser for kinetic measurement of serum IgG. Clin. Chem. 1974; 30: 1320
   Google Scholar
• Buffone G. J., Savory J., Cross R. E., Hammond J. E. Evaluation of kinetic light scattering as an approach to the measurement of specifc proteins with the centrifugal analyser. I. Methodology. Clin. Chem. 1975; 21: 1731
   PubMed Web of Science ®Google Scholar
• Buffone G. J., Cross R. E., Savory J., Soodok C. Measurement of laser induced near front surface light scattering with a parallel fast analyser system. Anal. Chem. 1974; 46: 2047
   Web of Science ®Google Scholar
• Buffone G. J., Heintges M. G., Savory J., Killingsworth L. M. The kinetic nephelometric measurement of IgG and albumin in serum and CSF using a laser modified Aminco Autochem centrifugal fast analyser. Clin. Chem. 1975; 21: 943
   Web of Science ®Google Scholar
• Junge J. M., Junde C. O., Krebs E. G. A study of antibody-antigen reaction rates by light transmission methods. Arch. Biochem. Biophys. 1955; 55: 338
   Google Scholar
• Goodman M., Ramsey D. S., Simpson W. L., Demp D. G., Basinski D. H., Brennan M. J. The use of chicken antiserum for the rapid determination of plasma protein components. J. Lab. Clin. Med 1957; 45: 151
   Google Scholar
• Ritchie R. F. A simple direct and sensitive technique for the measurement of specific proteins in dilute solution. J. Lab. Clin. Med. 1967; 70: 512
   PubMed Web of Science ®Google Scholar
• Kahan J., Sundblad L. Automated immunochemical determination of -lipoproteins, in Tehnicon Int. Symp. Automation in Analytical Chemistry. Medaid Inc., New York 1967; Vol. 2: 361, 1966
   Google Scholar
• Kahan J., Sundblad L. Immunochemical determination of -lipoprotein. Scand. J. Clin. Lab. Invest. 1969; 24: 61
   PubMed Web of Science ®Google Scholar
• Blom M., Sorensen D. A turbidimetric continuous flow system for immunochemical quantitation of blood proteins by use of a modified photometer. Clin. Chem. 1973; 19: 1148
   PubMedGoogle Scholar
• Van Munster P. J. J., Heelen G. E.J. M., Samuel-Mantigh M., Holtman Van Meurs M. A turbidimetric immunoassay (TIA) with automated individual blank compensation. Clin. Chim. Acta 1977; 76: 377
   PubMedGoogle Scholar
• Bergstrom K., Lefvert A. K. An automated turbidimetric immunoassay for plasma proteins. Scand J. Clin. Lab. Invest. 1980; 40: 637
   PubMed Web of Science ®Google Scholar
• Spencer K., Price C. P. Kinetic immunoturbidimetric measurement of thyroxine binding globulin. Clin. Chem. 1980; 26: 1531
   PubMed Web of Science ®Google Scholar
• Malkas H., Buschbaum P., Castro A. An automated turbidimetric rate method for immunoglobulin assays. Clin. Chim. Acta 1978; 88: 523
   PubMedGoogle Scholar
• Blom M., Hjorne N. Immunochemical determination of serum albumin with a centrifugal analyser. Clin. Chem. 1975; 21: 195
   PubMed Web of Science ®Google Scholar
• Blom M., Hjorne N. Profile analysis of blood proteins with a centrifugal analyser. Clin. Chem. 1978; 22: 657
   Google Scholar
• Finley P. R., Williams R. J., Byers J. M. Immunochemical determination of human immunoglobulins with a centrifugal analyser. Clin. Chem. 1978; 22: 1037
   Google Scholar
• Dito W. R. Rapid immunonephelometric quantitation of eleven serum proteins by centrifugal fast analyser. Am. J. Clin. Pathol 1979; 71: 301
   PubMed Web of Science ®Google Scholar
• Spencer K., Price C. P. The use of the IL Multistat III centrifugal analyser for kinetic immunoturbidimetry. The measurement of serum transferrin. Centrifugal Analysers in Clinical Chemistry, C. P. Price, K. Spencer. Praeger, New York 1980; 457
   Google Scholar
• Wenham P. R., Horn D. D. Determination of serum/plasma albumin by kinetic turbidimetry using the Rotochem Ha centrifugal fast analyser. Centrifugal Analysers in Clinical Chemistry, C. P. Price, K. Spencer. Praeger, New York 1980; 477, 109a.
   Google Scholar
• Fu P. C., Zic V. An automated bichromatic measurement of serum immunoglobulins. Ann. Clin. Lab. Sci 1978; 8: 323, 109b.
   PubMedGoogle Scholar
• Marell G. J., Brombacker P. J. Rapid and sensitive determination of immunoglobulins by centrifugal analyser. J. Clin. Chem. Clin. Biochem. 1981; 19: 67
   PubMedGoogle Scholar
• Ritchie R. F. Reference materials for plasma protein analysis. Automated Immunoanalysis Part I, R. F. Ritchie. Marcel Dekker, New York 1978; 159
   Google Scholar
• Grubb A. Immunochemical quantitation of IgG. Influences of the antiserum and of the antigenic population. Scand. J. Clin. Lab. Invest. 1973; 31: 465
   PubMed Web of Science ®Google Scholar
• Alper C. A., Rosen F. S. Clinical applications of complement assays. Adv. Int. Med. 1975; 20: 61
   PubMedGoogle Scholar
• Perrin L. H., Lambert P. H., Miescher P. A. Complement breakdown products in plasma from patients with systemic lupus erythromatosis and patients with membranoproliferative glomerulonephritis. J. Clin. Invest. 1975; 56: 165
   PubMed Web of Science ®Google Scholar
• Havez R. Laboratory experience and results in the determination of immunoglobulins and haptoglobin in an automated system. Automated Immunoprecipitaion Reactions, J. P. Ham. Technicon Instrument Corp., Tarrytown, NY 1972; 18: 259
   Google Scholar
• Seneviratne C. S., Moores S. Kinetic turbidimetric determination of serum immunoglobulins using a Multistat III centrifugal analyser. Centrifugal Analysers in Clinical Chemistry, C. P. Price, K Spencer. Praeger, New York 1980; 449
   Google Scholar
• Whicher J. T. Consideratione della immunogiobulini. Eslratto Clin. Lab. 1980; 4: 295
   Google Scholar
• Gilliland B. C. Immunological quantitation of serum immunoglobulins. Am. J. Clin. Pathol. 1977; 68: 664
   PubMed Web of Science ®Google Scholar
• Shenkin A., Morrison B., Robertson D. A. Some problems in the correction for intrinsic light scattering of samples in specific protein analysis by automated immunoprecipitation. Ann. Clin. Biochem. 1977; 14: 163
   PubMedGoogle Scholar
• Webster D. A study of the interaction of bromocresol green with isolated serum globulin fractions. Clin. Chim. Acta 1974; 53: 109
   PubMed Web of Science ®Google Scholar
• Gustaffson J. C. Improved specificity of serum albumin determination and estimation of acute phase reactants by use of the bromocresol green reaction. Clin. Chem. 1976; 22: 616
   PubMedGoogle Scholar
• Pinnell A. E., Northam B. E. New automated dye binding method for serum albumin determination with bromocresol purple. Clin. Chem. 1978; 24: 80
   PubMed Web of Science ®Google Scholar
• Diagneault R., Vernet-Nyssen M. Transferrin. AutomatedImmunoanalysis Part 1, R. F. Ritchie. Marcel Dekker, New York 1978; 253
   Google Scholar
• Standing S., Price C. P. A kinetic method for the determination of haptoglobin as haemoglobin binding capacity. Clin. Chim. Acta 1976; 66: 393
   PubMedGoogle Scholar
• Harmoinen A., Perko M., Gronroos P. Rapid quantitative determination of C-reactive protein using an LKB 8600 reaction rate analyser. Clin. Chim. Acta 1981; 111: 117
   PubMed Web of Science ®Google Scholar
• Ritchie R. F., Alper C. A., Graves J., Pearson M., Larson C. Automated quantitation of proteins in serum and other biological fluids. Am. J. Clin. Pathol 1973; 59: 151
   PubMed Web of Science ®Google Scholar
• Alper C. A., Ritchie R. F. Comparison of immunochemical techniques. Automated Immunoanalysis Part 1, R. F. Ritchie. Marcel Dekker, New York 1978; 139
   Google Scholar
• Reimer C. B., Maddison S. E. Standardisation of human immunoglobulin quantitation. A review of current states and problems. Clin. Chem. 1976; 22: 577
   PubMedGoogle Scholar
• Whicher J. T., Hunt J., Perry D. E., Hobbs J. R., Fifield R., Keyser J., Kohn J., Riches P., Smith A. M., Thompson R. A., Ward A. M., White P. Method-specific variations in the calibration of a new immunoglobulin standard suitable for use in nephelometric techniques. Clin. Chem. 1978; 24: 531
   PubMed Web of Science ®Google Scholar
• Buttner J., Borth R., Boutwell J. H., Broughton P. M. G., Bowyer R.C. Approved recommendations on quality control in clinical chemistry, Part I: General principles and terminology. Clin. Chim. Acta. 1979; 98: I29F
   Google Scholar
• Ingle J. D., Crouch S. R. Evaluation of quantitative molecular absorbtion spectrophotometric measurement. Anal. Chem. 1972; 44: 1375
   Web of Science ®Google Scholar
• Pardue H. L., Hewitt T. E., Milano M. J. Photometric errors in equilibrium and kinetic analyses based on absorbtion spectroscopy. Clin. Chem. 1974; 20: 1028
   PubMed Web of Science ®Google Scholar
• Renner E., Heinecke G., Lange H. Clinical value of renal protein clearance determination. Contr. Nephrol. 1975; 1: 134
   PubMedGoogle Scholar
• Link H., Tibbling G. Principles of albumin and IgG analyses in neurological disorders 111: Evaluation of IgG synthesis within the central nervous system. Scand. J. Clin. Lab. Invest. 1977; 37: 397
   PubMed Web of Science ®Google Scholar
• Thompson E. J. Immunochemistry of CSF proteins. Immunochemistry in Clinical Laboratory Medicine, A. M. Ward, J. T. Whicher. MTP Press, LancasterEngl 1979; 229
   Google Scholar
• Turner M. W., Rowe D. S. A naturally occurring fragment related to the heavy chains of immunoglobulin G in normal human urine. Nature 1966; 210: 130
   PubMedGoogle Scholar
• Bernard A., Buchet J. P., Roels H., Masson P., Lauwerys R. Renal excretion of proteins and enzymes in workers exposed to cadmium. Eur. J. Clin. Invest. 1979; 9: 11
   PubMed Web of Science ®Google Scholar
• Maclight G. M., Stuckey S. E., Cabamillas F. F., Keating M. J., Tourtellotte W. W., Schild C, Freireich E. G. Diagnosis of leukaemia and lymphoma in the central nervous system by ft-microglobulin determination, JV. Engl. J. Med. 1980; 303: 718
   PubMedGoogle Scholar
• Lizana J., Evrin P. E., Hellsing K. Automated immunonephelometric determination of β2-microglobulin in urine. Clin. Chem. 1974; 20: 894
   Google Scholar
• O'Reily D. S., Whicher J., Sanderson R. A simple precise and sensitive nephelometric array for β2-microglobulin in body fluids. J. Immunol. Methods 1982, in press
   Google Scholar
• Vincent W. F., Harris E. W., Yaverbaum S. The estimation of precipitating antibody using a tubridimetric technique. Immunology 1970; 18: 143
   PubMedGoogle Scholar
• Davies G. E. The uses of a sensitive micronephelometer in the estimation of antigens and precipitating antibodies. Immunology 1971; 20: 779
   PubMedGoogle Scholar
• Hellsing K., Richter W. Immunochemical quantitation of dextran by a polymer-enhanced nephelometric procedure. J. Immunol Methods 1974; 5: 147
   PubMedGoogle Scholar
• Riccomi H, Masson P. L., Vaerman J. P., Heremans J. F. An automated nephelometric inhibition immunoassay (NINIA) for haptens, Colloq. AIP, Brussels. 1972; 9
   Google Scholar
• Pauling L., Pressman D., Gronberg A. Serological properties of simple substances. VII. Quantitative theory of inhibition of haptens of precipitation of heterogeneous antisera with antigens, and comparison with experimental results for polyhaptenin simple substances and for azoproteins. J. Am. Chem. Soc 1944; 66: 784
   Google Scholar
• Cambiaso C. L., Riccomi H. A., Masson P. L., Heremans J. F. Automated nephelometric immunoassay. 11. Its application to the determination of hapten. J. Immunol. Methods 1974; 5: 293
   PubMedGoogle Scholar
• Gauldie J., Sherrington E., Sircar P. K. Automated nephelometric inhibition immunoassay of digoxin and morphine. Fed. Proc. 1975; 104: 34
   Google Scholar
• Nishikawa T., Kubott Saito M. Competitive nephelometric immunoassay for theophylline in plasma. Clin. Chim. Acta 1979; 91: 59
   PubMedGoogle Scholar
• Nishikawa T., Kubott Saito M. Competitive nephelometric immunoassay for antiepileptic drugs in patient blood. J. Immunol. Methods. 1979; 29: 85
   PubMedGoogle Scholar
• Finley P. R., Dye J. A., Williams J., Lichti D. A. Rate nephelometric inhibition immunoassay of phenytoin and phenobarbitol. Clin. Chem. 1981; 27: 405
   PubMedGoogle Scholar
• Cheng A., Bray K., Polito A. Nephelometric inhibition assay for Gentamycin. Clin. Chem. 1979; 25: 1078
   Google Scholar
• Pranis R., Stenglein K., Reran E. Therapeutic drug-monitoring of Dilantin (phenytoin) utilising nephelometric inhibition immunoassay. Clin. Chem. 1979; 25: 1095
   Google Scholar
• Kottgen E., Bauer C, Gerok W. Laser nephelometry of lectin-glycoprotein complexes: a new method for their quantitation and differentiation. Anal. Biochem. 1979; 96: 391
   PubMedGoogle Scholar
• Warren C, Whicher J., Kohn J. The use of concanavalin A to measure acute phase proteins by laser nephelometry. J. Immunol. Methods 1980; 32: 141
   PubMedGoogle Scholar
• Martin M. F. R., Dieppe P. A., Jones H. E., Warren C, Whicher J. T., Kohn J. Serum concanavalin A binding in rheumatoid arthritis. Ann. Rheum. Dis. 1982; 41: 133
   PubMedGoogle Scholar
• Galanos C, Freudenberg M. A., Luderitz O., Rietschel E. T., Vestphal O. Chemical, physicochemical and biological properties of bacterial lipopolysaccharides. Prog. Clin. Biol. Res. 1979; 29: 321
   PubMedGoogle Scholar
• Bang F. B. A bacterial disease of Limulus polyphemus. Bull. Johns Hopkins Hasp. 1956; 98: 325
   PubMedGoogle Scholar
• Laurent P. H., Zeller H. Formation des gels-etude nephelometrique laser application aux endotoxines bacteriennes, in C. R. 2nd Reunion Natl. Groupe d'Etudes sur Applications de la Nephelomelre Laser. Hoechst-Behring, Paris 1979; 25
   Google Scholar
• Nishi H. H., Kestner J., Elin R. J. A new semi-automated nephelometric procedure for the determination of bacterial endotoxin. Clin. Chem. 1579; 25: 1106
   Google Scholar
• Total Protein in Urine. Instrument Information, Hyland Div. Travenol Laboratories, Costa Mesa, Calif.
   Google Scholar
• Lafay S., Diemert M. C., Galli J. Etude comparative de deux methodes de dosage des proteins dans le urine et le LCR, in C.R. 2nd Reunion Natl. Groupe d'Etudes sur Applications de la Nephelomelre Laser 1979; 72: 432
   Google Scholar
• Finley P. R., Hicks J. M., Williams R. J., Hinlickey J., Lichti D. A. Rate nephelometric measurement of rheumatoid factor in serum. Clin. Chem. 1909; 25, 1979
   Google Scholar
• Roberts-Thompson P. J., Bradley J. A nephelometric study of the reaction of monoclonal rheumatoid factor with heat aggregated gamma globulin and sera from patients with immune complex disease. Clin. Exp. Immunol. 1979; 37: 408
   PubMedGoogle Scholar
• Grabner W., Bergner D., Sailer D., Berg G. Untersuchungen zur zuverlassigkent quantitativer immunoglobulibestimmugen (IgG, IgA, IgM) durche einfache radiale immunodiffusion. Clin. Chim. Acta 1972; 39: 59
   PubMedGoogle Scholar
• Borel-Giraud N., Maillawin A., Vernet-Nyssen M. Dosage de l'alpha-1-foetoproteine serique par electroimmunodiffusion sur agarose. Clin. Chim. Acta 1976; 71: 117
   PubMedGoogle Scholar
• Gill C. W., Bush W., Burleigh W. M., Fischer C. L. An evaluation of a C-reactive protein assay using a rate immunonephelometric procedure. Am. J. Clin. Pathol. 1981; 75: 50
   PubMedGoogle Scholar
• Kagedal B., Kallberg M. Determination of thyroxine binding globulin in human serum by single radial immunodiffusion and radioimmunoassay. Clin. Chem. 1977; 23: 1694
   PubMed Web of Science ®Google Scholar
• Macdonald D. J., Nicol K. M., Belfield A., Shah M. M., Mack D. S. Enzyme linked immunoassay for placental lactogen in human serum. Clin. Chem. 1980; 26: 745
   PubMedGoogle Scholar
• Chard T., Sykes A. Fluoroimmunoassay for human choriomammotrophin. Clin. Chem. 1979; 25: 973
   PubMedGoogle Scholar