Changes in plasma membrane glycoproteins of rat spermatozoa during maturation in the epididymis.

作者: C R Brown , K I von Glos , R Jones

DOI: 10.1083/JCB.96.1.256

关键词:

摘要: Glycoproteins on the plasma membrane of testicular and cauda epididymidal spermatozoa have been labeled with galactose oxidase/NaB [3H]4 sodium metaperiodate/NaB[3H]4, followed by analysis SDS polyacrylamide gels. The major glycoprotein labeling has a molecular weight 110,000 whereas greater than 90% radio-label is incorporated into proteins 32,000. These 32,000-mol wt X are homologous similar purified from epididymal secretion which shown previously to be synthesized in caput epididymidis under hormonal control. Immunofluorescence revealed that present flagellum mature but not immature they patchy distribution suggesting mobile within plane membrane. membrane-bound possess hydrophobic domains as charge-shift electrophoresis also label lipophilic photoaffinity probe contact lipid bilayer. evidence indicates there considerable reorganization structure during maturation epididymis some changes brought about direct interaction secretory proteins.

参考文章(43)
W H J Ward, P Britton, S van Heyningen, The hydrophobicities of cholera toxin, tetanus toxin and their components Biochemical Journal. ,vol. 199, pp. 457- 460 ,(1981) , 10.1042/BJ1990457
Theodore L. Steck, Glyn Dawson, Topographical Distribution of Complex Carbohydrates in the Erythrocyte Membrane Journal of Biological Chemistry. ,vol. 249, pp. 2135- 2142 ,(1974) , 10.1016/S0021-9258(19)42808-1
A. Lewis Farr, Oliver H. Lowry, Rose J. Randall, Nira J. Rosebrough, Protein Measurement with the Folin Phenol Reagent Journal of Biological Chemistry. ,vol. 193, pp. 265- 275 ,(1951)
W.D. Gathmann, David Aminoff, Steric factors involved in the action of glycosidases and galactose oxidase. Biochemical and Biophysical Research Communications. ,vol. 103, pp. 68- 76 ,(1981) , 10.1016/0006-291X(81)91661-2
A. Helenius, K. Simons, Charge shift electrophoresis: simple method for distinguishing between amphiphilic and hydrophilic proteins in detergent solution. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 74, pp. 529- 532 ,(1977) , 10.1073/PNAS.74.2.529
James K. Koehler, P. Gaddum-Rosse, Media induced alterations of the membrane associated particles of the guinea pig sperm tail. Journal of Ultrastructure Research. ,vol. 51, pp. 106- 118 ,(1975) , 10.1016/S0022-5320(75)80012-8
Diana Gold Myles, Paul Primakoff, Anthony R. Bellvé, Surface domains of the guinea pig sperm defined with monoclonal antibodies Cell. ,vol. 23, pp. 433- 439 ,(1981) , 10.1016/0092-8674(81)90138-0