Cloning and tissue distribution of human membrane-bound aminopeptidase P

Richard C. Venema, Hong Ju, Rong Zou, Virginia J. Venema, James W. Ryan

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

Complementary DNA clones encoding human membrane-bound aminopeptidase P (AMP) were isolated by reverse transcription-polymerase chain reaction (RT- PCR) of human kidney and lung poly (A)+ RNA. Comparison of the human AmP sequence to that of the pig shows significant evolutionary divergence with only 83% amino acid sequence identity between the two species. Northern hybridization analysis and RT-PCR suggests that the soluble and membrane- bound forms of human AmP are products of two distinct genes or, through alternative splicing, have different C-terminal sequences.

Original languageEnglish (US)
Pages (from-to)45-48
Number of pages4
JournalBiochimica et Biophysica Acta - Gene Structure and Expression
Volume1354
Issue number1
DOIs
StatePublished - Oct 1 1997

Fingerprint

Cloning
Tissue Distribution
Organism Cloning
Tissue
Membranes
Polymerase chain reaction
Alternative Splicing
Transcription
Complementary DNA
Genes
Amino Acids
Polymerase Chain Reaction
Messenger RNA
Reverse Transcription
Amino Acid Sequence
Swine
Clone Cells
Kidney
Lung
X-Pro aminopeptidase

Keywords

  • Aminopeptidase P
  • Bradykinin

ASJC Scopus subject areas

  • Biochemistry
  • Genetics
  • Structural Biology
  • Biophysics

Cite this

Cloning and tissue distribution of human membrane-bound aminopeptidase P. / Venema, Richard C.; Ju, Hong; Zou, Rong; Venema, Virginia J.; Ryan, James W.

In: Biochimica et Biophysica Acta - Gene Structure and Expression, Vol. 1354, No. 1, 01.10.1997, p. 45-48.

Research output: Contribution to journalArticle

Venema, Richard C. ; Ju, Hong ; Zou, Rong ; Venema, Virginia J. ; Ryan, James W. / Cloning and tissue distribution of human membrane-bound aminopeptidase P. In: Biochimica et Biophysica Acta - Gene Structure and Expression. 1997 ; Vol. 1354, No. 1. pp. 45-48.
@article{42d8f7b64df243e2ab28d15fd80b2df2,
title = "Cloning and tissue distribution of human membrane-bound aminopeptidase P",
abstract = "Complementary DNA clones encoding human membrane-bound aminopeptidase P (AMP) were isolated by reverse transcription-polymerase chain reaction (RT- PCR) of human kidney and lung poly (A)+ RNA. Comparison of the human AmP sequence to that of the pig shows significant evolutionary divergence with only 83{\%} amino acid sequence identity between the two species. Northern hybridization analysis and RT-PCR suggests that the soluble and membrane- bound forms of human AmP are products of two distinct genes or, through alternative splicing, have different C-terminal sequences.",
keywords = "Aminopeptidase P, Bradykinin",
author = "Venema, {Richard C.} and Hong Ju and Rong Zou and Venema, {Virginia J.} and Ryan, {James W.}",
year = "1997",
month = "10",
day = "1",
doi = "10.1016/S0167-4781(97)00126-7",
language = "English (US)",
volume = "1354",
pages = "45--48",
journal = "Biochimica et Biophysica Acta - Gene Structure and Expression",
issn = "0167-4781",
publisher = "Elsevier BV",
number = "1",

}

TY - JOUR

T1 - Cloning and tissue distribution of human membrane-bound aminopeptidase P

AU - Venema, Richard C.

AU - Ju, Hong

AU - Zou, Rong

AU - Venema, Virginia J.

AU - Ryan, James W.

PY - 1997/10/1

Y1 - 1997/10/1

N2 - Complementary DNA clones encoding human membrane-bound aminopeptidase P (AMP) were isolated by reverse transcription-polymerase chain reaction (RT- PCR) of human kidney and lung poly (A)+ RNA. Comparison of the human AmP sequence to that of the pig shows significant evolutionary divergence with only 83% amino acid sequence identity between the two species. Northern hybridization analysis and RT-PCR suggests that the soluble and membrane- bound forms of human AmP are products of two distinct genes or, through alternative splicing, have different C-terminal sequences.

AB - Complementary DNA clones encoding human membrane-bound aminopeptidase P (AMP) were isolated by reverse transcription-polymerase chain reaction (RT- PCR) of human kidney and lung poly (A)+ RNA. Comparison of the human AmP sequence to that of the pig shows significant evolutionary divergence with only 83% amino acid sequence identity between the two species. Northern hybridization analysis and RT-PCR suggests that the soluble and membrane- bound forms of human AmP are products of two distinct genes or, through alternative splicing, have different C-terminal sequences.

KW - Aminopeptidase P

KW - Bradykinin

UR - http://www.scopus.com/inward/record.url?scp=0030710551&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030710551&partnerID=8YFLogxK

U2 - 10.1016/S0167-4781(97)00126-7

DO - 10.1016/S0167-4781(97)00126-7

M3 - Article

C2 - 9375790

AN - SCOPUS:0030710551

VL - 1354

SP - 45

EP - 48

JO - Biochimica et Biophysica Acta - Gene Structure and Expression

JF - Biochimica et Biophysica Acta - Gene Structure and Expression

SN - 0167-4781

IS - 1

ER -