State Modifications of Thymocyte Plasma Membrane Proteins and Lipids by Mitogenic Doses of Concanavalin A: A Raman Study on Isolated Membrane Vesicles

References

• Wallach D. F.H. Membrane Molecular Biology of Neoplastic Cells. Elsevier Scientific Publishing Company, Amsterdam 1975; 435–481, Chapter 10
   Google Scholar
• Resch K. Membrane Associated Events in Lymphocyte Activation. Receptors and Recognition, P. Cuatrecasas, M. F. Greaves. Series A, No. 1, Chapman and Hall, London 1976; 59–118, Chapter 3
   Google Scholar
• Loor F. Structure and Dynamics of the Lymphocyte surface in relation to differentiation, recognition and activation. Progress in Allergy, Vol. 23. S. Karger, Basel 1977; 1–153
   Google Scholar
• Schmidt-Ullrich R., Wallach D. F.H. Cooperativity in concanavalin A-binding to thymocyte membranes: Correlation with polymerization of a receptor glycoprotein. Biochem. Biophys. Res. Commun. 1976; 69: 1011–1018
   PubMedGoogle Scholar
• Bornens M., Karsenti E., Avrameas S. Cooperative binding of Concanavalin A to Thymocytes at 4°C and Micro-redistribution of Concanavalin A Receptors. Eur. J. Biochem. 1976; 65: 61–69
   PubMedGoogle Scholar
• Schmidt-Ullrich R., Wallach D. F.H., Hendricks J. Interaction of Concanavalin A with rabbit thymocyte plasma membranes. Distinction between low-affinity associations and positively cooperative binding mediated by a specific glycoprotein. Biochim. Biophys. Acta 1976; 443: 587–600
   Google Scholar
• Wallach D. F.H., Schmidt-Ullrich R. Isolation of plasma membrane vesicles from animal cells. Methods in Cell Biology 1977; 15: 235–276
   Google Scholar
• Schmidt-Ullrich R., Mikkelsen R. B., Wallach D. F.H. Transmembrane disposition of the 55,000-dalton concanavalin A receptor protein of thymocyte plasma membranes. J. Biol. Chem. 1978; 253: 6973–6978
   Google Scholar
• Schmidt-Ullrich R., Verma S. P., Wallach D. F.H. Concanavalin A stimulation modifies the lipid and protein structure of rabbit thymocyte plasma membranes: A laser-Raman study. Biochim. Biophys. Acta 1976; 426: 477–488
   Google Scholar
• Verma S. P., Wallach D. F.H. Multiple thermotropic state transitions in erythrocyte membranes: a laser-Raman study of CH-stretching regions and acoustical regions. Biochim. Biophys. Acta 1976; 436: 307–318
   PubMedGoogle Scholar
• Verma S. P., Schmidt-Ullrich R., Thompson W. S., Wallach D. F.H. Differences between the structural dynamics of plasma membranes of normal hamster lymphocytes and lymphoid cells neoplastically transformed by simian virus 40 as revealed by laser Raman spectroscopy. Cancer Res. 1977; 37: 3490–3493
   Google Scholar
• Verma S. P., Wallach D. F.H. Erythrocyte membranes undergo cooperative, pH-sensitive state transitions in the physiological-temperature range: evidence from laser Raman spectroscopy. Proc. Natl. Acad. Sci. USA 1976; 73: 355–361
   Google Scholar
• Mikkelsen R. B., Verma S. P., Wallach D. F.H. Effect of transmembrane ion gradient on the Raman spectra of sealed hemoglobin-free erythrocyte membrane vesicles. Proc. Natl. Acad. Sci. USA 1978; 75: 5478–5482
   PubMedGoogle Scholar
• Verma S. P., Wallach D. F.H. Raman spectra of some saturated, unsaturated and deuterated C18 -fatty acids in the CH-deformation and CH-stretching regions. Biochim. Biophys. Acta 1977; 486: 217–227
   PubMed Web of Science ®Google Scholar
• Graber B., Peticolas W. L. On the quantitative interpretation of biomembrane structure by Raman spectroscopy. Biochim. Biophys. Acta 1977; 465: 260–274
   Google Scholar
• Snyder R. G., Hsu S. L., Krimm G. Vibrational spectra in the C-H stretching region and the structure of the polymethylene chain. Spectrochimica Acta 1978; 34A: 395–406
   Web of Science ®Google Scholar
• Mendelsohn R., Maisano J. Use of deuterated phospholipids on Raman spectroscopic studies of membrane structure I. Multilayers of dimyristoyl phosphatidylcholine and its -d54, derivative, with distearoyl phosphatidylcholine. Biochim. Biophys. Acta 1973; 506: 192–201
   Google Scholar
• Verma S. P., Wallach D. F.H. Effect of melittin on thermotropic lipid state transitions in phosphatidylcholine liposomes. Biochim. Biophys. Acta 1976; 426: 616–623
   Google Scholar
• Bunow M. R., Leyin I. W. Comment on the carbon-hydrogen stretching region of vibrational Raman spectra of phos-pholipids. Biochim. Biophys. Acta 1977; 487: 388–394
   PubMed Web of Science ®Google Scholar
• Curatolo W., Sakura J. D., Small D. M., Shipley G. Protein-lipid interactions; Recombinants of the proteolipid apoprotein of myelin with dimyristoyl lecithin. Biochemistry 1977; 16: 2313–2319
   Google Scholar
• Curatolo W., Verma S. P., Sakura J. D., Small D. M., Shipley G. G., Wallach D. F.H. Structural effects of myelin proteolipid apoprotein on phospholipids: A Raman spectroscopic study. Biochemistry 1978; 17: 1802–1807
   Google Scholar
• Kang S. Y., Gutowsky H. S., Hsung J. C., Jacobs R., King T. E., Rice D., Oldfield E. Nuclear magnetic investigation of the cytochrome oxidase-phospholipid interaction: A new model for boundary lipid-biochemistry. Biochemistry 1979; 18: 3257–3267
   Google Scholar
• Kang S. Y., Gutowsky H. S., Oldfield E. Spectroscopic studies of specifically deuterium labeled membrane systems. Nuclear Magnetic Resonance Investigation of Protein-lipid interactions in Escherichia Coli membranes. Biochemistry 1979; 18: 3268–3272
   Google Scholar
• Verma S. P., Wallach D. F.H. Changes of Raman-scattering in CH-stretching region during thermally-induced unfolding of ribonuclease. Biochem. Biophys. Res. Commun. 1977; 74: 472–479
   Google Scholar
• Borochov H., Shinitzky M. Vertical displacement of membrane proteins mediated by changes in microviscosity. Proc. Natl. Acad. Sci. 1976; 73: 4526–4530
   PubMed Web of Science ®Google Scholar
• Shinitzky M., Rivnay B. Degree of Exposure of Membrane proteins determined by fluorescence quenching. Biochemistry 1977; 16: 982–989
   PubMed Web of Science ®Google Scholar
• Tanford C. Protein denaturation. Part C. Theoretical models for the mechanism of denaturation. Advances in Protein Chemistry, C. B. Anjinsen, Jr., J. T. Edsall, F. M. Richards. Academic Press, NY 1970; Vol. 2A: 1–108
   Google Scholar
• McLendon G., Radany E. Is protein turnover thermodynamically controlled. J. Biol. Chem. 1978; 253: 6335–6337
   PubMed Web of Science ®Google Scholar
• Schmidt-Ullrich R., Wallach D. F.H., Ferber E. Concanavalin A augments the turnover of electrophoretically defined thymocyte plasma membrane proteins. Biochim. Biophys. Acta 1974; 356: 288–299
   Google Scholar