Characterization of the major cyanogen bromide fragment of alpha-A crystallin.
Alpha crystallin from the bovine lens has been digested with cyanogen bromide, and the major fragment (CB-1) has been purified using reverse phase HPLC. Characterization of this fragment by Edman degradation and antisera to synthetic peptides indicates that it originates from alpha-A crystallin, but lacks the N-terminal methionine and the last 35 amino acids from the C-terminus of the molecule. The purified CB-1 fragment binds as well as native alpha crystallin to lens membrane, but is unable to self-assemble into the correct size of high molecular weight oligomeric complexes characteristic of the intact alpha-A chain. Together, these results demonstrate that the alpha-A chain is comprised of at least two functional domains, one of which is involved in binding of alpha-A crystallin to lens membrane, and another which is necessary for correct self-assembly of the molecule into high molecular weight oligomers.
Ifeanyi
F
F
Division of Biology, Kansas State University, Manhattan 66506.
Takemoto
L
L
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002462:Cell Membrane / Q000378:metabolism; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D003459:Crystallins / Q000032:analysis* / Q000378:metabolism; D003488:Cyanogen Bromide; D004591:Electrophoresis, Polyacrylamide Gel; D007908:Lens, Crystalline / Q000378:metabolism; D010446:Peptide Fragments / Q000032:analysis* / Q000378:metabolism
D003459:Crystallins; D010446:Peptide Fragments; D003488:Cyanogen Bromide