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The assay of Met-enkephalin aminopeptidase with [125I]Met-enkephalin

descriptionPublicationkeyboard_double_arrow_right Article 01 Jun 1982Publisher:Elsevier BVJournal:Journal of Biochemical and Biophysical Methods, volume 6, pages 133-139 (issn: 0165-022X,

Authors: James L. Caffrey; Donald H. Hodges;

doi: 10.1016/0165-022x(82)90059-8

pmid: 7108125

The assay of Met-enkephalin aminopeptidase with [125I]Met-enkephalin

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Abstract

Presented here are procedural modifications which permit the utilization of 125I-labeled Met-enkephalin as substrate in the assay of rat brain enkephalin aminopeptidase. Th hydrolysis of enkephalin is monitored by the release of [125I]tyrosine separated on Porapak Q. The release of tyrosine is proportionate with both increasing time and tissue concentration. The estimated Km is near 10(-4) M and the enzyme activity can be inhibited more than 95% with puromycin. The majority of the enzyme activity remains in the 100,000 x g supernatant following differential centrifugation.

Related Organizations

College of Osteopathic Medicine of the Pacific
United States

Keywords

Time Factors, Enkephalin, Methionine, Hydrolysis, Brain, Enkephalins, Aminopeptidases, Rats, Kinetics, Centrifugation, Density Gradient, Methods, Animals, Tyrosine, Puromycin, Endorphins

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Fields of Science (3) View all

medical and health sciences

basic medicine

Fields of Science

medical and health sciences

basic medicine

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Neuroscience

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