Primary structure of the snake venom L-amino acid oxidase shows high homology with the mouse B cell interleukin 4-induced Fig1 protein

被引：56

作者：

Raibekas, AA ^{[1
]}

Massey, V ^{[1
]}

机构：

[1] Univ Michigan, Dept Biol Chem, Ann Arbor, MI 48109 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1998年 / 248卷 / 03期

关键词：

D O I：

10.1006/bbrc.1998.9024

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：

The 2.8-kb sequence of cDNA encoding southeastern diamondback rattlesnake venom L-amino acid oxidase was determined. A translated single open reading frame revealed a 58.7-kDa polypeptide containing a signal sequence and FAD binding motif. The protein similarity search and analysis showed that the snake L-amino acid oxidase possesses the highest degree of homology (37% of identity) with a protein encoded by the mouse B cell interleukin 4-induced Fig1 gene. (C) 1998 Academic Press.

引用

页码：476 / 478

页数：3

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