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Science 22 June 1979:
Vol. 204. no. 4399, pp. 1323 - 1326
DOI: 10.1126/science.377484
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Articles

Science, Vol 204, Issue 4399, 1323-1326
Copyright © 1979 by American Association for the Advancement of Science

articles

An extrinsic membrane polypeptide associated with high-molecular-weight protein aggregates in human cataract

A Spector, MH Garner, WH Garner, D Roy, P Farnsworth, and S Shyne

A 43,000-dalton polypeptide has been isolated from the high-molecular-weight disulfide-rich fraction of the water-insoluble protein of human cataractous lenses. On the basis of immunochemical reactivity and fluorescent antibody binding, this polypeptide is localized in the membrane region of the lens cell. This observation suggests an interaction between the soluble lens proteins and membrane-associated polypeptides in the formation of large protein aggregates which may cause cataract.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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M. G. Friedrich and R. J. W. Truscott (2009)
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{alpha}B-crystallin: A Golgi-Associated Membrane Protein in the Developing Ocular Lens.
R. K. Gangalum and S. P. Bhat (2009)
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Early Glycation Products Produce Pentosidine Cross-links on Native Proteins. NOVEL MECHANISM OF PENTOSIDINE FORMATION AND PROPAGATION OF GLYCATION.
P. Chellan and R. H. Nagaraj (2001)
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