Micro-method to isolate and purify amyloid proteins for chemical characterization

References

• Pras M, Schubert M, Zucker-Franklin D, Rimon A, Franklin E C. The characterization of soluble amyloid prepared in water. J Clin Invest 1968; 47: 924–933
   PubMed Web of Science ®Google Scholar
• Glenner G G, Terry W, Harada M, Isersky C, Page D. Amyloid fibril protein: Proof of homology with immunoglobulin light chains by sequence analysis. Science 1971; 172: 1150–1151
   PubMed Web of Science ®Google Scholar
• Westermark P. The pathogenesis of amyloidosis: understanding general principles. Amer J Path 1998; 152: 1125–1127
   PubMed Web of Science ®Google Scholar
• Castaño E M, Prelli F, Morelli L, Avagnina A, Kahn A, Frangione B. Immunoglobulin lambda light chains are the precursors of ureteral localized amyloidosis: a mi-cromethod for extraction of amyloid. Amyloid: Int J Exp Clin Invest 1997; 4: 253–258
   Web of Science ®Google Scholar
• Olsen K E, Sletten K, Westermark P. Extended analysis of AL-amyloid protein from abdominal wall subcutaneous fat biopsy: kappa IV immunoglobulin light chain. Biochem Biophys Res Comm 1998; 245: 713–716
   PubMed Web of Science ®Google Scholar
• Kaplan B, German G, Pras M. Isolation and characterization of amyloid proteins using milligram amounts of amyloid-containing tissue. J Liq Chromatogr 1993; 16(11)2249–2268
   Web of Science ®Google Scholar
• Kaplan B, German G, Ravid M, Pras M. Determination of amyloid type by ELISA using milligram amounts of tissue. Clin Chim Acta 1994; 229: 171–179
   PubMed Web of Science ®Google Scholar
• Yakar S, Kaplan B, Livneh A, Martin B, Miura K, Ali-Khan Z, Shtrasburg S, Pras M. Direct evidence for SAA deposition in tissues during murine amyloidogenesis. Scand J Immunol 1994; 40: 653–658
   PubMed Web of Science ®Google Scholar
• Kaplan B, Yakar S, Kumar A, Pras M, Gallo G. Immunochemical characterization of amyloid in diagnostic biopsy tissues. Amyloid: Int J Exp Clin Invest 1997; 4: 80–86
   Web of Science ®Google Scholar
• Kaplan B, Vidal R, Kumar A, Ghiso J, Frangione B, Gallo G. Amino-terminal identity of co-existent amyloid and non-amyloid immunoglobulin K light chain deposits. A human disease to study alterations of protein conformation. Clin Exp Immunol 1997; 110: 472–478
   PubMed Web of Science ®Google Scholar
• Kaplan B, Haroutunian V, Koudinov A, Patael Y, Pras M, Gallo G. Biochemical assay for amyloid P deposits to distinguish Alzheimer's disease from other dementias. Clin Chim Acta 1999; 280: 147–159
   PubMed Web of Science ®Google Scholar
• Kaplan B, Hrncic R, Murphy C L, Gallo G, Weiss D T, Solomon A. Microextraction and purification techniques applicable to the chemical characterization of amyloid proteins in minute amounts of tissue. Methods in Enzymology, R Wetzel. Academic Press, San Diego, Boston, London, Sydney, Tokyo, Toronto 1999; vol. 309: 67–81
   Google Scholar
• Kaplan B, Pras M. Separation of amyloid proteins by size-exclusion chromatography in aqueous organic mobile phase. J Liq Chromatogr 1992; 15(14)2467–2486
   Web of Science ®Google Scholar
• Pras M, Zaretsky J, Frangione B, Franklin E C. AA protein in case of “primary” or “idiopathic” amyloidosis. Am J Med 1980; 68: 291–294
   PubMed Web of Science ®Google Scholar
• Prelli F, Pras M, Frangione B. Degradation and deposition of amyloid fibrils are tissue specific. Biochemistry 1987; 26: 8351–8256
   Web of Science ®Google Scholar
• Prelli F, Pras M, Shtrasburg S, Frangione B. B. Characterization of high molecular weight amyloid A proteins. Scand J Immunol 1991; 33: 783–786
   PubMed Web of Science ®Google Scholar
• Pras M, Prelli F, Franklin E C, Frangione B. Primary structure of an amyloid prealbumin variant in familial polyneuropathy of Jewish origin. Proc Nat Acad Sci USA 1983; 80: 539–542
   PubMed Web of Science ®Google Scholar
• Yuen S W, Chui A H, Wilson K J, Yuan P M. Microanalysis of SDS-PAGE electroblotted proteins. Applied Biosysterns User Bulletin 36. Foster City, CA 1988; 1–17
   Google Scholar
• Harrington M G. Elution of proteins from gels. Methods in Enzymology, M P Deutscher. Academic Press, San Diego, New York, Berkeley, Boston, Sydney, Tokyo, Toronto 1990; vol 182: 488–495
   Google Scholar
• Patterson S D, Aebersold R. Mass spectrometric approaches for the identification of gel-separated proteins. Electrophoresis 1995; 16: 1791–1814
   PubMed Web of Science ®Google Scholar
• Corran P H. Reversed-phase chromatography of proteins. HPLC ofmacromolecules. A Practical Approach, R WA Oliver. Oxford University Press, Oxford, New York, Tokyo 1991; 127–157
   Google Scholar
• Kaplan B. Application of polyacrylamide slab gel electrophoresis to the analysis and small-scale purification of amyloid proteins. Anal Chim Acta 1998; 372: 161–172
   Web of Science ®Google Scholar
• Kaplan B, Pras M. Preparative fractionation of amyloid proteins on a microgram scale by high-performance liquid chromatography and polyacrylamide gel electrophoresis. Clin Chim Acta 1987; 163: 199–205
   PubMed Web of Science ®Google Scholar
• Kaplan B, Pras M, Ravid M. Isolation and purification of amyloid protein A by sodium dodecyl sulphate polyacrylamide gel electrophoresis and reverse phase high performance liquid chromatography. J Chromatogr 1992; 573: 17–22
   PubMed Web of Science ®Google Scholar
• Kaplan B, Yakar S, Balta Y, Pras M, Martin B. Isolation and purification of two major serum amyloid A isotypes SAA1 and SAA2 from the acute phase plasma of mice. J Chromatogr 1997; 704: 69–76
   Web of Science ®Google Scholar
• Stone K L, LoPresti M B, Crawford J M, DeAngelis R, Williams K R. Reverse-phase HPLC separation of subnanomole amounts of peptides obtained from enzymatic digests. HPLC of Peptides and Proteins: Separation, Analysis and Conformation, C Mant, R S Hodges. CRC Press, Boca Raton, Fl 1991; 669–677
   Google Scholar
• Kaplan B, Pras M. Removal of sodium dodecyl sulfate from proteins by gel permeation chromatography. J Chromatogr 1987; 423: 376–379
   PubMed Web of Science ®Google Scholar
• Weber K, Kutter J. Reversible denaturation of enzymes by sodium dodecyl sulfate. J Biol Chem 1971; 246: 4505–4509
   Web of Science ®Google Scholar
• Kapp O M, Vinogradov S N. Removal of sodium dodecyl sulfate from proteins. Anal Biochem 1978; 91: 230–235
   PubMed Web of Science ®Google Scholar
• Henderson L E, Oroszlan S, Konigsberg W. A micromethod for complete removal of dodecyl sulfate from proteins by ion-pair extraction. Anal Biochem 1979; 93: 153–157
   PubMed Web of Science ®Google Scholar
• Stone K, Williams K R. Enzymatic digestion of proteins and HPLC peptide isolation. A Practical Guide to Protein and Peptide Purification for Microsequencing, 2^d, P Matsudaira. Academic Press, San Diego, Boston, London, Sydney, Tokyo, Toronto 1993; 45–73
   Google Scholar
• Parekh B S, Mehta H B, West M D, Moteralo R C. Preparative elution of proteins from nitrocellulose membranes after separation by sodium dodecyl sulphate - polyacrylamide gel electrophoresis. Anal Biochem 1985; 148: 87–92
   PubMed Web of Science ®Google Scholar
• Szewszyk B, Summers D F. Preparative elution of proteins blotted in immobilon membranes. Anal Biochem 1988; 168: 48–53
   PubMed Web of Science ®Google Scholar
• Le Gendre N, Mansfield M, Weiss A, Matsudaira P. Purification of proteins and peptides by SDS-PAGE. A Practical Guide to Protein and Peptide Purification for Microsequencing, 2^nd ed., P Matsudaira. Academic Press, San Diego, Boston, London, Sydney, Tokyo, Toronto 1993; 45–73
   Google Scholar
• Lee K H, Harrington M G. Preparative gel electrophoresis. Gel Electrophoresis of Proteins. A Practical Approach, 3^rd ed., B D Hames. Oxford University Press, Oxford, New York, Tokyo 1998; 93–104
   Google Scholar
• Westermark P. The heterogeneity of protein AA in secondary (reactive) systemic amyloidosis. Biochim Biophys Actal 1982; 701: 19–23
   PubMed Web of Science ®Google Scholar
• Husby G, Marhaug G, Dowton B, Sletten K, Sipe J D. Serum amyloid A (SAA); biochemistry, genetics and the pathogenesis of AA amyloidosis. Amyloid: Int J Exp Clin Invest 1994; 1: 119–137
   Web of Science ®Google Scholar
• Solomon A, Weiss D T, Schell M, Hrncic R, Murphy C L, Wall J, McGavin M D, Pan H J, Kabalka G W, Paulus M J. Transgenic mouse model of AA amyloidosis. Amer J Path 1999; 154: 1267–1272
   PubMed Web of Science ®Google Scholar
• Kisilevsky R, Lemieux L J, Fraser P E, Kong X, Hultin P G, Szarek W A. Arresting amyloidosis in vivo, using small-molecule anionic sulphonates or sulphates: implications for Alzheimer's disease. Nat Med 1995; 1: 143–148
   PubMed Web of Science ®Google Scholar
• Patterson S D. Matrix-assisted laser-desorption/ion-ization mass spectrometric approaches for the identification of gel-separated proteins in the 5–50. pmol range. Electrophoresis 1995; 16: 1104–1114
   PubMed Web of Science ®Google Scholar
• Patterson S D. From electrophoretically separated protein to identification: strategies for sequence and mass analysis. Anal Biochem 1994; 221: 1–15
   PubMed Web of Science ®Google Scholar
• Kaplan B. Gel electrophoresis in protein and peptide analysis. Encyclopedia of Analytical Chemistry: Instrumentation and Application, R Meyers. Wiley & Sons. 2000, in press
   Google Scholar