Antisera to synthetic peptides as probes of structural changes during aging of alpha-crystallin from the bovine lens.
Polyclonal antisera have been made to synthetic peptides of 11-15 residues that correspond to nine different regions of the alpha A crystallins. These antisera have been used in a radioimmunoassay to quantitatively probe for structural and/or covalent changes of alpha-crystallins in the nucleus versus cortex of the adult bovine lens. Antisera specific for the C-terminal and N-terminal regions of the alpha-crystallins bind more to alpha-crystallins from cortex. Antisera to three out of the seven internal sequences (residues 75-89, 87-101 and 135-149) bind better to alpha-crystallins from the bovine lens nucleus, suggesting a greater accessibility of these sequences to antisera binding. Together, these studies demonstrate that antisera against synthetic peptide sequences of alpha A crystallins are very specific probes that can detect structural and/or covalent changes in specified regions of the alpha-crystallins during the process of aging in the bovine lens.
Takemoto
L
L
Division of Biology, Kansas State University, Manhattan 66506.
Emmons
T
T
Granstrom
D
D
Jacobs
S
S
D000375:Aging; D000595:Amino Acid Sequence; D000818:Animals; D000918:Antibody Specificity; D001666:Binding Sites, Antibody; D002417:Cattle; D003459:Crystallins / Q000502:physiology*; D007106:Immune Sera; D007908:Lens, Crystalline / Q000032:analysis / Q000254:growth & development*; D015335:Molecular Probes; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000276:immunology*; D011487:Protein Conformation
D003459:Crystallins; D007106:Immune Sera; D015335:Molecular Probes; D010446:Peptide Fragments