LOSS OF THE C-TERMINAL SERINE RESIDUE FROM BOVINE BETA-B-2-CRYSTALLIN

被引：13

作者：

KILBY, GW ^{[1
]}

CARVER, JA ^{[1
]}

ZHU, JL ^{[1
]}

SHEIL, MM ^{[1
]}

TRUSCOTT, RJW ^{[1
]}

机构：

[1] UNIV WOLLONGONG,DEPT CHEM,AUSTRALIAN CATARACT RES FDN,WOLLONGONG,NSW 2522,AUSTRALIA

来源：

EXPERIMENTAL EYE RESEARCH | 1995年 / 60卷 / 05期

基金：

澳大利亚研究理事会;

关键词：

ELECTROSPRAY MASS SPECTROMETRY; BETA-B-2-CRYSTALLIN; ALPHA-CRYSTALLIN; TANDEM MASS SPECTROMETRY;

D O I：

10.1016/S0014-4835(05)80061-2

中图分类号：

R77 [眼科学];

学科分类号：

100212 ;

摘要：

Electrospray mass spectrometric (ES-MS) examination of bovine beta-crystallins showed a significant component corresponding in mass to beta B-2-crystallin less one serine residue. Tryptic digestion, followed by isolation and characterisation of the C-terminal peptide, demonstrated that this new species has arisen by the loss of the C-terminal serine residue. This phenomenon appears to be age-related since no truncation was detected in beta B-2-crystallin from foetal lenses and the proportion of the truncated form, as judged by ES-MS, was lower in beta-crystallin isolated from calf lenses than that from the lenses of 3-year-old animals. This process therefore is similar to a recently reported loss of the C-terminal serine from alpha-A-crystallin, which we have confirmed using ES-MS. Loss of a C-terminal serine from both crystallins may indicate the presence of carboxypeptidase-A-like activity in bovine lenses. ES-MS data provided no evidence for a significant degree of phosphorylation of beta B-2-crystallin.

引用

页码：465 / 469

页数：5