PRIMARY STRUCTURE OF V-ATPASE SUBUNIT-B FROM MANDUCA-SEXTA MIDGUT

被引：39

作者：

NOVAK, FJS

GRAF, R

WARING, RB

WOLFERSBERGER, MG

WIECZOREK, H

HARVEY, WR

机构：

[1] TEMPLE UNIV,DEPT BIOL,PHILADELPHIA,PA 19122

[2] UNIV MUNICH,INST ZOOL,W-8000 MUNICH 2,GERMANY

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1992年 / 1132卷 / 01期

关键词：

VACUOLAR ATPASE; PLASMA MEMBRANE; CDNA SEQUENCE; TOBACCO HORNWORM; LEPIDOPTERA; INSECT; LARVA;

D O I：

10.1016/0167-4781(92)90053-3

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 amino acid sequence of a vacuolar-type ATPase (V-ATPase) subunit B has been deduced from a cDNA clone isolated from a Manduca sexta larval midgut library. The library was screened by hybridization with a labeled cDNA encoding subunit B of Arabidopsis thaliana tonoplast V-ATPase. The M. sexta V-ATPase subunit B consists of 494 amino acids with a calculated M(r) of 54902. The amino acid sequence deduced for V-ATPase subunit B of M. sexta is between 98% and 76% identical with that of seven other V-ATPase subunits B and > 52% identical with three archaebacterial ATPase subunits B.

引用

页码：67 / 71

页数：5

共 44 条

[11]

DENDA K, 1988, J BIOL CHEM, V263, P17251

[12] URINARY ACIDIFICATION IN TURTLE BLADDER IS DUE TO A REVERSIBLE PROTON-TRANSLOCATING ATPASE [J].