CLONING AND SEQUENCE-ANALYSIS OF THE HUMAN LIVER RHODANESE - COMPARISON WITH THE BOVINE AND CHICKEN ENZYMES

被引：23

作者：

PALLINI, R

GUAZZI, GC

CANNELLA, C

CACACE, MG

机构：

[1] CNR,CTR STUDIO CELLULE GERMINALI,VIA TOMMASO PENDOLA 62,I-53100 SIENA,ITALY

[2] UNIV SIENA,FAC MED CHIR,IST SCI NEUROL,I-53100 SIENA,ITALY

[3] UNIV ROME LA SAPIENZA,FAC MED CHIR,IST SCI ALIMENTAZ,I-00185 ROME,ITALY

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 180卷 / 02期

关键词：

D O I：

10.1016/S0006-291X(05)81148-9

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 cDNA for the human rhodanese (thiosulfate: cyanide sulfurtransferase, EC 2.8.1.1), a nuclearly encoded protein of the mitochondrial matrix, was isolated from a human fetal liver cDNA library. Nucleotide sequence revealed an open reading frame coding for a polypeptide of 295 amino acids, which presented a 57% and 58% identity with the bovine and avian rhodanese, respectively. The analysis of the 5′-ends of the coding region gave no evidence for the presence of a cleavable signal sequence as found in other mitochondrial proteins. A comparison with two available amino acid sequences (cow and chicken) showed that sequence similarity is not restricted to the α-helices and β-structures motifs which are remarkably superimposable in the two halves of bovine rhodanese, but extends to adjacent regions. © 1991 Academic Press, Inc.

引用

页码：887 / 893

页数：7

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