THE PRIMARY STRUCTURE OF THE LARGER SUBUNIT OF SOLUBLE GUANYLYL CYCLASE FROM BOVINE LUNG - HOMOLOGY BETWEEN THE 2 SUBUNITS OF THE ENZYME

被引：105

作者：

KOESLING, D ^{[1
]}

HARTENECK, C ^{[1
]}

HUMBERT, P ^{[1
]}

BOSSERHOFF, A ^{[1
]}

FRANK, R ^{[1
]}

SCHULTZ, G ^{[1
]}

BOHME, E ^{[1
]}

机构：

[1] EUROPEAN MOLEC BIOL LAB,W-6900 HEIDELBERG,GERMANY

来源：

FEBS LETTERS | 1990年 / 266卷 / 1-2期

关键词：

Amino acid sequence; cDNA sequence; Soluble guanylyl cyclase;

D O I：

10.1016/0014-5793(90)81523-Q

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 primary structure of the larger subunit of the soluble guanylyl cyclase from bovine lung, which catalyzes the formation of cyclic GMP from GTP, has been determined. Two clones, isolated from two bovine libraries yielded a total of 3261 bp with a coding region of 2073 bp. The open reading frame encodes a protein of 691 amino acids and a molecular mass of 77 500. The deduced amino acid sequence reveals regions which are, to a large extent, homologous to the sequence of the smaller subunit of the enzyme as well as to the sequences of other gyanylyl and adenylyl cyclases. © 1990.

引用

页码：128 / 132

页数：5

共 25 条

[1] MICROPREPARATIVE SEPARATION OF PEPTIDES DERIVED FROM SODIUM DODECYL SULFATE-SOLUBILIZED PROTEINS [J].