Age-dependent deamidation of αB-crystallin

• Published in: FEBS letters Vol. 322; no. 1; pp. 69 - 72
• Main Authors: Groenen, Patricia J.T.A., van Dongen, Maria J.P., Voorter, Christina E.M., Bloemendal, Hans, de Jong, Wilfried W.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 03.05.1993; Elsevier
• Subjects: Aged; Aged, 80 and over; Aging - metabolism; Amides - metabolism; Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Animals; Asparagine - metabolism; Biological and medical sciences; Cattle; Crystallins - metabolism; Deamidation; Fundamental and applied biological sciences. Psychology; Humans; Lens; Miscellaneous; Molecular aging; Molecular Sequence Data; Peptide Mapping; Proteins; Racemization; αB-Crystallin; Racemization; Lens; Deamidation; αB-Crystallin; Molecular aging; Proteins; Site specificity; Chemical modification; Crystallin; Correlation analysis; Beta-Peptide chain; Age

Bovine and human αB-crystallin undergo deamidation upon aging in the lens. In bovine αB-crystallin, the specific site of dearnidation has been identified by peptide mapping after tryptic digestion. Asn-146 was found to be subject to deamidation, whereas the only other asparagine residue, at position...