Species variation in pulmonary endothelial aminopeptidase P activity.

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Article

Species variation in pulmonary endothelial aminopeptidase P activity.

The Journal of pharmacology and experimental therapeutics - 1 Dec 1991

Chen X, Orfanos S E, Ryan J W, Chung A Y, Hess D C, Catravas J D

Abstract excerpt

Pulmonary endothelial aminopeptidase P (AmP) may be an important contributor to the inactivation of circulating bradykinin in certain species. To examine this possibility, we measured AMP activity in vivo and in vitro using Arg-Pro-Pro-[3H]benzylamide (3H-APPB) as substrate under conditions of first order enzyme kinetics. Utilizing multiple indicator dilution techniques, metabolism of 3H-APPB to Arg and...

Topics

Aminopeptidases
Animals
Cats
Cattle
Cells, Cultured
Endothelium, Vascular
Female
Genetic Variation
Humans
Kidney
Kinetics
Lung

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Male

Pulmonary Artery

Rabbits

Rats

Rats, Inbred Strains

Species Specificity

Source

Open in PubMed

Identifiers

PMID: 1762077

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1762077-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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