Involvement of the N-terminal region in alpha-crystallin-lens membrane recognition.
Previous studies have demonstrated that alpha-crystallin binds specifically, in a saturable manner, to lens membrane. To determine the region of the alpha-crystallin molecule that might be involved in this binding, native alpha-crystallin from the bovine lens has been treated by limited digestion with trypsin, to produce alpha-A molecules with an intact C-terminal region, and a nicked N-terminal region. Compared to intact alpha-crystallin, trypsin-treated alpha-crystallin binds less avidly to lens membrane, suggesting that the N-terminal region of the alpha-A molecule may play a key role in the recognition between lens membrane and crystallin.
Division of Biology, Kansas State University, Manhattan 66506.
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Ifeanyi
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Takemoto
D000818:Animals; D015153:Blotting, Western; D002417:Cattle; D003459:Crystallins / Q000032:analysis*; D007904:Lens Cortex, Crystalline / Q000378:metabolism*; D010443:Peptide Chain Termination, Translational; D010446:Peptide Fragments / Q000378:metabolism; D011485:Protein Binding; D014357:Trypsin
D003459:Crystallins; D010446:Peptide Fragments; D014357:Trypsin