OXIDATION OF THE N-TERMINAL METHIONINE OF LENS ALPHA-A CRYSTALLIN

被引：53

作者：

TAKEMOTO, L ^{[1
]}

HORWITZ, J ^{[1
]}

EMMONS, T ^{[1
]}

机构：

[1] UNIV CALIF LOS ANGELES,SCH MED,JULES STEIN EYE INST,LOS ANGELES,CA 90024

来源：

CURRENT EYE RESEARCH | 1992年 / 11卷 / 07期

关键词：

D O I：

10.3109/02713689209000738

中图分类号：

R77 [眼科学];

学科分类号：

100212 ;

摘要：

Antiserum against the N-terminal peptide of bovine alpha-A crystallin has been used to monitor purification of two different sero-positive peptides (i.e. Tla and Tlb) from a tryptic digest of bovine lens proteins. Both these peptides have similar amino acid compositions, but peptide Tlb has a molecular weight 16 atomic mass units larger than Tla, suggesting posttranslational modification. Analysis of ionization fragments of the Tlb peptide by mass spectrometry demonstrates that this difference in molecular weight is due to the in vivo oxidation of the N-terminal met residue of the alpha-A crystallin molecule.

引用

页码：651 / 655

页数：5

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