Purification of a Membrane-Bound Metalloendopeptidase from Porcine Kidney That Degrades Peptide Hormones

A porcine kidney microsomal metalloendopeptidase has been enriched 3900-fold. Gel filtration on a calibrated Toyo-Soda G-3000 SW column indicated an approximate molecular weight for the endopeptidase of 88,000± 2000. The purified enzyme is inhibited by a number of synthetic inhibitors of thermolysin...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1981-11, Vol.78 (11), p.6623-6627
Main Authors: Mumford, Richard A., Pierzchala, Patricia A., Strauss, Arnold W., Zimmerman, Morris
Format: Article
Language:English
Subjects:
Animals
Biochemistry
Chromatography
Endopeptidases - isolation & purification
Endopeptidases - metabolism
Enzymes
Flow velocity
Gels
Hormones
Kidney - enzymology
Kidneys
Kinetics
Metalloendopeptidases
Metalloproteins - isolation & purification
Metalloproteins - metabolism
Microsomes
Microsomes - enzymology
Molecular Weight
P branes
Substrate Specificity
Swine
Zinc
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Summary:A porcine kidney microsomal metalloendopeptidase has been enriched 3900-fold. Gel filtration on a calibrated Toyo-Soda G-3000 SW column indicated an approximate molecular weight for the endopeptidase of 88,000± 2000. The purified enzyme is inhibited by a number of synthetic inhibitors of thermolysin. The endopeptidase hydrolyzes the succinyl (Suc)-containing fluorogenic peptide substrate Suc-Ala-Ala-Phe-(7-amino-4-methylcoumarin) at the Ala-Phe position with a Kmof 2.0× 10-4M. The endopeptidase also hydrolyzes a variety of peptides including corticotropin, substance P, angiotensin I and II, neurotensin, somatostatin, bradykinin, and the renin tetradecapeptide substrate. The endopeptidase hydrolyzes both [Leu]- and [Met]enkephalin at the Gly-Phe bond.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.78.11.6623