STUDIES ON BETA-CRYSTALLIN FROM PRIMATE LENS

  • 1 January 1976
    • journal article
    • research article
    • Vol. 15  (8) , 673-677
Abstract
The major .beta.-crystallin fractions from the human lens and the lenses of other selected primates [Macaca mulatta, Saimiri sciureus, Miopithecus talapoin, Pan troglodytes, Lemur fulvus fulvus and Galago senegalensis] were isolated and partially characterized. Primate .beta.-crystallins, like those of most other mammals, consisted of 2 heterogeneous protein fractions (.beta.H and .beta.L) of quite different molecular size. Most of the polypeptide chains comprising the .beta.H and .beta.L heteropolymers were common to both fractions. Primate .beta.H-crystallin may be smaller than .beta.H from other vertebrate species. Human .beta.H contained a major component on sodium dodecyl sulfate (SDS) electrophoresis which was much larger (about 60,000 daltons) than other .beta.-crystallin polypeptides. Immunochemical evidence indicated that some components of primate .beta.-crystallin evolved rapidly, although at least 1 antigenic component was very conservative and gave a reaction of identity with all other vertebrate .beta.-crystallins studied.

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