Cloning and functional expression of the cytoplasmic form of rat aminopeptidase P

被引：14

作者：

Czirják, G

Burkhart, WA

Moyer, MB

Antal, J

Shears, SB

Enyedi, P

机构：

[1] Semmelweis Univ Med, Dept Physiol, H-1444 Budapest, Hungary

[2] Glaxo Res Inst, Res Triangle Pk, NC 27709 USA

[3] Agr Biotechnol Ctr, ACE Lab, H-2101 Godollo, Hungary

[4] NIEHS, Inositol Lipid Sect, Lab Signal Transduct, NIH, Res Triangle Pk, NC 27709 USA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION | 1999年 / 1444卷 / 03期

基金：

匈牙利科学研究基金会;

关键词：

aminopeptidase P; cDNA cloning; functional expression; cytoplasmic;

D O I：

10.1016/S0167-4781(99)00005-6

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：

A rat cytoplasmic aminopeptidase P was purified from liver cytosol with a procedure including an affinity elution step with 3 mu M inositol 1,3,4-trisphosphate. Proteolytic fragments were generated, sequenced and the enzyme was cloned from a rat liver cDNA library. The structure shows high (87.8% and 95.5%, respectively) sequence identity at the nucleotide and amino acid levels with the previously described human putative cytoplasmic aminopeptidase P. The cloned rat enzyme was functionally expressed in Escherichia coli and also in COS-1 cells. Western blot analysis, using an antibody generated against the recombinant protein, and Northern blot hybridization showed ubiquitous expression of the protein in different tissues with the highest expression level in the testis. (C) 1999 Elsevier Science B.V. All rights reserved.

引用

页码：326 / 336

页数：11

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