Novel Activity of Human Angiotensin I Converting Enzyme: Release of the NH2- and COOH-Terminal Tripeptides from the Luteinizing Hormone-Releasing Hormone

Angiotensin I converting enzyme (ACE; kininase II; peptidyldipeptide hydrolase, EC 3.4.15.1) cleaves COOH-terminal dipeptides from active peptides containing a free COOH terminus. We investigated the hydrolysis of luteinizing hormone-releasing hormone (LH-RH) by homogeneous human ACE. Although this...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 1985-02, Vol.82 (4), p.1025-1029
Hauptverfasser:	Skidgel, Randal A., Erdos, Ervin G.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino acids Analytical, structural and metabolic biochemistry Biochemistry Biological and medical sciences Chemical Phenomena Chemistry Chlorides Enzymes Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Gonadotropin-Releasing Hormone Hormones Humans Hydrolases Hydrolysis In Vitro Techniques Kidney - enzymology Kinetics Luteinization Median eminence Oligopeptides Peptidyl-Dipeptidase A - metabolism Sodium Chloride Substrate Specificity Table salt
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Zusammenfassung:	Angiotensin I converting enzyme (ACE; kininase II; peptidyldipeptide hydrolase, EC 3.4.15.1) cleaves COOH-terminal dipeptides from active peptides containing a free COOH terminus. We investigated the hydrolysis of luteinizing hormone-releasing hormone (LH-RH) by homogeneous human ACE. Although this decapeptide is blocked at both the NH2and COOH termini, it was metabolized to several peptides, which were separated by HPLC and identified by amino acid analysis. A major product was the NH2-terminal tripeptide,
ISSN:	0027-8424 1091-6490
DOI:	10.1073/pnas.82.4.1025