Multiple molecular forms of rat brain enkephalinase

Robert S. Rush, Louis B. Hersh

Research output: Contribution to journalArticlepeer-review

19 Scopus citations


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.

Original languageEnglish
Pages (from-to)445-451
Number of pages7
JournalLife Sciences
Issue number5
StatePublished - 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.

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology (all)
  • Pharmacology, Toxicology and Pharmaceutics (all)


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