Multiple molecular forms of rat brain enkephalinase

Robert S. Rush; Louis B. Hersh

doi:10.1016/0024-3205(82)90329-0

Multiple molecular forms of rat brain enkephalinase

Robert S. Rush, Louis B. Hersh

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19 Scopus citations

Abstract

Rat brain enkephalinase has been partially purified by ion exchange chromatography, chromatofocusing, and affinity chromatography on immobilized lectins. Ion exchange chromatography resolved two principle forms of enkephalinase designated A₁ and A₂. Both enkephalinase A₁ and A₂ are bound to immobilized lentil lectin while chromatography on immobilized wheat germ lectin resolved each of the principle forms into two subforms, A_1,1, A_1,2, A_2,1, and A_2,2. All four enkephalinase forms have similar, if not identical kinetic properties. The possible implications of multiple molecular forms of enkephalinases are discussed.

Original language	English
Pages (from-to)	445-451
Number of pages	7
Journal	Life Sciences
Volume	31
Issue number	5
DOIs	https://doi.org/10.1016/0024-3205(82)90329-0
State	Published - Aug 2 1982

Bibliographical note

Funding Information:
We thank Mr. Michael Faull-Mltas for h~s technical assistance. This study was supported in part by Gra~t No. 02243 from NIDA and Grant No. 1-391 from The Robert A. Welch Foundation, Houston, Texas.

Funding

We thank Mr. Michael Faull-Mltas for h~s technical assistance. This study was supported in part by Gra~t No. 02243 from NIDA and Grant No. 1-391 from The Robert A. Welch Foundation, Houston, Texas.

Funders	Funder number
National Institute on Drug Abuse	1-391
Welch Foundation

ASJC Scopus subject areas

General Pharmacology, Toxicology and Pharmaceutics
General Biochemistry, Genetics and Molecular Biology

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10.1016/0024-3205(82)90329-0

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title = "Multiple molecular forms of rat brain enkephalinase",

abstract = "Rat brain enkephalinase has been partially purified by ion exchange chromatography, chromatofocusing, and affinity chromatography on immobilized lectins. Ion exchange chromatography resolved two principle forms of enkephalinase designated A1 and A2. Both enkephalinase A1 and A2 are bound to immobilized lentil lectin while chromatography on immobilized wheat germ lectin resolved each of the principle forms into two subforms, A1,1, A1,2, A2,1, and A2,2. All four enkephalinase forms have similar, if not identical kinetic properties. The possible implications of multiple molecular forms of enkephalinases are discussed.",

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note = "Funding Information: We thank Mr. Michael Faull-Mltas for h~s technical assistance. This study was supported in part by Gra~t No. 02243 from NIDA and Grant No. 1-391 from The Robert A. Welch Foundation, Houston, Texas.",

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AU - Hersh, Louis B.

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AB - Rat brain enkephalinase has been partially purified by ion exchange chromatography, chromatofocusing, and affinity chromatography on immobilized lectins. Ion exchange chromatography resolved two principle forms of enkephalinase designated A1 and A2. Both enkephalinase A1 and A2 are bound to immobilized lentil lectin while chromatography on immobilized wheat germ lectin resolved each of the principle forms into two subforms, A1,1, A1,2, A2,1, and A2,2. All four enkephalinase forms have similar, if not identical kinetic properties. The possible implications of multiple molecular forms of enkephalinases are discussed.

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Multiple molecular forms of rat brain enkephalinase

Abstract

Bibliographical note

Funding

ASJC Scopus subject areas

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