Site‐specific racemization in aging α‐crystallin

FEBS Letters

Groenen, Patricia J.T.A.¹  Voorter, Christina E.M.¹  Bloemendal, Hans¹  de Jong, Wilfried W.¹  van den Ijssel, Paul R.L.A.¹ 

[1] Department of Biochemistry, Centre of Eye Research, University of Nijmegen, P.O. Box 9101, 6500 HB Nijmegen, The Netherlands

关键词: Lens;    Crystallin;    Racemization;    Molecular aging;   

DOI  :  10.1016/0014-5793(90)81131-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Of all aspartyl residues in bovine αA-crystallin, only Asp-151 exhibits pronounced racemization. Asp-151 is also one of the sites where peptide bond cleavage occurs in in vivo aging αA-crystallin. This aspartyl residue is followed by an alanyl residue and resides in a flexible carboxyl terminal extension of α-crystallin. Both in vivo and in vitro racemization studies indicate that the pronounced and site-specific racemization of Asp-151 proceeds via formation of a succinimide intermediate. The in vivo racemization of aspartyl residues in αA-crystallin is discussed with regard to the proposed tertiary structure of α-crystallin.

【 授权许可】

Unknown