SITE-SPECIFIC RACEMIZATION IN AGING ALPHA-A-CRYSTALLIN

被引:58
作者
GROENEN, PJTA [1 ]
VANDENIJSSEL, PRLA [1 ]
VOORTER, CEM [1 ]
BLOEMENDAL, H [1 ]
DEJONG, WW [1 ]
机构
[1] CATHOLIC UNIV NIJMEGEN,DEPT BIOCHEM,CTR EYE RES,POB 9101,6500 HB NIJMEGEN,NETHERLANDS
关键词
Crystallin; Lens; Molecular aging; Racemization;
D O I
10.1016/0014-5793(90)81131-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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. © 1990.
引用
收藏
页码:109 / 112
页数:4
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