PRIMARY STRUCTURE OF THE 2 VARIANTS OF XENOPUS-LAEVIS MTSSB, A MITOCHONDRIAL-DNA BINDING-PROTEIN

被引：29

作者：

GHRIR, R

LECAER, JP

DUFRESNE, C

GUERIDE, M

机构：

[1] UNIV PARIS 11,INST GENET & MICROBIOL,BIOL GEN LAB,BATIMENT 400,F-91405 ORSAY,FRANCE

[2] CNRS,PHYSIOL NERVEUSE LAB,SERV COMMUN MICROSEQUENCAGE,F-91198 GIF SUR YVETTE,FRANCE

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 1991年 / 291卷 / 02期

关键词：

D O I：

10.1016/0003-9861(91)90152-9

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 single-stranded DNA binding protein from Xenopus laevis oocyte mitochondria (mtSSB) has been determined by Edman degradation of the intact molecule and peptides derived from partial α-chymotrypsin proteolysis and enzymatic cleavage with trypsin and endoproteinase Glu-C. The native mtSSB is composed of two related polypeptide chains, mtSSBs and mtSSBr. The sequence of mtSSBs consists of 129 amino acids with a calculated molecular mass of 14,627 Da. Comparison of the first 80 residues of the two chains reveals 91% identity. A high degree of similarity is found between mtSSB and Escherichia coli SSB or F sex factor SSB. © 1991.

引用

页码：395 / 400

页数：6

共 14 条

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