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Zvi Vogel

We have characterized two distinct brain enzymatic activities which hydrolyze Leu-enkephalin (Leu-Enk). One, a puromycin-sensitive aminopeptidase, fails to cleave the enkephalin analog (D-Ala2)Met-Enk amide, Its specific activity is reduced upon purification of synaptosomal membranes. The second enzyme is a particulate endopeptidase cleaving Leu-Enk at the Gly-Phe peptide bond (Ksbm 2.2×10-5M) to yield Tyr-Gly-Gly and Phe-Leu. (D-Ala2)Met-Enk amide is hydrolyzed by this enzyme although at a lower rate compared to that of Leu-Enk. The endopeptidase cosediments with the synaptosomal membranes. It can be released from the membranes into the high-speed supernatant by the use of Triton X-100. In contrast to the aminopeptidase, the endopeptidase is not inhibited by puromycin or mercurybenzoate but is effectively inhibited by barbiturates.

Proceedings of the International Narcotic Research Club Conference, June 11–15, 1979, North Falmouth, Massachusetts, USA

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DEGRADATION OF ENKEPHALIN BY TWO BRAIN ENZYMATIC ACTIVITIES

Zvi Vogel

DEGRADATION OF ENKEPHALIN BY TWO BRAIN ENZYMATIC ACTIVITIES

We have characterized two distinct brain enzymatic activities which hydrolyze Leu-enkephalin (Leu-Enk). One, a puromycin-sensitive aminopeptidase, fails to cleave the enkephalin analog (D-Ala2)Met-Enk amide, Its specific activity is reduced upon purification of synaptosomal membranes. The second enzyme is a particulate endopeptidase cleaving Leu-Enk at the Gly-Phe peptide bond (Ksbm 2.2×10-5M) to yield Tyr-Gly-Gly and Phe-Leu. (D-Ala2)Met-Enk amide is hydrolyzed by this enzyme although at a lower rate compared to that of Leu-Enk. The endopeptidase cosediments with the synaptosomal membranes. It can be released from the membranes into the high-speed supernatant by the use of Triton X-100. In contrast to the aminopeptidase, the endopeptidase is not inhibited by puromycin or mercurybenzoate but is effectively inhibited by barbiturates.

Proceedings of the International Narcotic Research Club Conference, June 11–15, 1979, North Falmouth, Massachusetts, USA

Scientific Publication
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