Cloning and tissue distribution of human membrane-bound aminopeptidase P

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

doi:10.1016/S0167-4781(97)00126-7

Cloning and tissue distribution of human membrane-bound aminopeptidase P

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

Graduate Studies

Research output: Contribution to journal › Article › peer-review

37 Scopus citations

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 language	English (US)
Pages (from-to)	45-48
Number of pages	4
Journal	Biochimica et Biophysica Acta - Gene Structure and Expression
Volume	1354
Issue number	1
DOIs	https://doi.org/10.1016/S0167-4781(97)00126-7
State	Published - Oct 1997

Keywords

Aminopeptidase P
Bradykinin

ASJC Scopus subject areas

Structural Biology
Biophysics
Biochemistry
Genetics

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10.1016/S0167-4781(97)00126-7

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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.}",

note = "Funding Information: This work was supported in part by a grant from the American Heart Association, Georgia Affiliate, Inc.",

year = "1997",

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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.

N1 - Funding Information: This work was supported in part by a grant from the American Heart Association, Georgia Affiliate, Inc.

PY - 1997/10

Y1 - 1997/10

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

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Cloning and tissue distribution of human membrane-bound aminopeptidase P

Abstract

Keywords

ASJC Scopus subject areas

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