HUMAN PEPTIDYLGLYCINE ALPHA-AMIDATING MONOOXYGENASE - CDNA, CLONING AND FUNCTIONAL EXPRESSION OF A TRUNCATED FORM IN COS CELLS

被引：59

作者：

GLAUDER, J

RAGG, H

RAUCH, J

ENGELS, JW

机构：

[1] UNIV FRANKFURT,INST ORGAN CHEM,W-6000 FRANKFURT 50,GERMANY

[2] HOECHST AG,W-6230 FRANKFURT 80,GERMANY

[3] UNIV FRANKFURT,INST BIOCHEM,W-6000 FRANKFURT,GERMANY

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 169卷 / 02期

关键词：

D O I：

10.1016/0006-291X(90)90366-U

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：

We have identified a cDNA encoding human peptidylglycine α-amidating monooxygenase (PAM; EC 1.14.17.3) with a total length of 3748 bp by screening of a human thyroid carcinoma lambda gt11 library using two heterologous oligonucleotides to conserved regions which derived from frog skin and bovine pituitary PAM sequences. Furthermore we have identified a sequence which differs in a 321 bp deletion. COS cells transfected with a truncated form of this cDNA (lacking the putative carboxyl-terminal transmembrane domain) generated a functional PAM that showed a 20-fold increase of the activity compared to the control and was visualized by immunoblotting. © 1990.

引用

页码：551 / 558

页数：8

共 23 条

[1] SECRETED ALPHA-AMIDATING ENZYMES ARE GENERATED BY SPECIFIC POSTTRANSLATIONAL PROCESSING OF PRECURSORS CONTAINING TRANSMEMBRANE DOMAINS [J].