Characterization of a neutral, divalent cation-sensitive endopeptidase: a possible role in neuropeptide processing.

S. Supattapone, S. M. Strittmatter, Lloyd D. Fricker, S. H. Snyder

Research output: Contribution to journalArticle

Abstract

A trypsin-like endopeptidase which cleaves the synthetic substrate Dansyl-Phe-Leu-Arg-Arg-Ala-Ser-Leu-Gly-COOH (Dansyl-Phe-Kemptide) primarily at the Arg4-Ala5 bond has been partially purified from bovine adrenal chromaffin granules, brain and liver. The enzyme appears to have a relatively homogeneous tissue distribution, although highest levels were found in brain regions such as the hippocampus and corpus striatum. Sucrose density gradient fractionation established that enzyme activity assayed at pH 8.5 is not associated with lysosomes. Purified enzyme displays a dimeric structure with subunit molecular weights of 40 kDa and 42 kDa and a native molecular weight of 85,000 Da. The endopeptidase has a neutral pH optimum, is sensitive to divalent cations and thiol reagents, and can cleave on either the amino or carboxyl side of some but not all internal basic amino acids.

Original languageEnglish (US)
Pages (from-to)173-181
Number of pages9
JournalBrain Research
Volume427
Issue number2
StatePublished - Apr 1988
Externally publishedYes

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Endopeptidases
Divalent Cations
Neuropeptides
kemptide
Enzymes
Molecular Weight
Chromaffin Granules
Corpus Striatum
Basic Amino Acids
Sulfhydryl Reagents
Brain
Tissue Distribution
Lysosomes
Trypsin
Sucrose
Hippocampus
Liver

ASJC Scopus subject areas

  • Neuroscience(all)

Cite this

Characterization of a neutral, divalent cation-sensitive endopeptidase : a possible role in neuropeptide processing. / Supattapone, S.; Strittmatter, S. M.; Fricker, Lloyd D.; Snyder, S. H.

In: Brain Research, Vol. 427, No. 2, 04.1988, p. 173-181.

Research output: Contribution to journalArticle

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