A novel neutral protease(s) from monkey liver

Kazuhiro Sogawa, Kenji Takahashi

    Research output: Contribution to journalArticlepeer-review

    6 Citations (Scopus)

    Abstract

    A novel neutral protease(s), which is presumably membrane-bound, was found in monkey liver using heat-denatured casein as a substrate and was separated from other major catheptic proteases by successive procedures of gel filtration on Ultrogel AcA 22, solubilization by deoxycholate and gel filtration on Sepharose 6B. The enzyme(s) showed maximal activity at pH 8.0, and was strongly inhibited by DFP and PMSF. Many other reagents tested, including TPCK, TLCK, pCMB, iodoacetic acid, and EDTA, were without marked effect on the activity. Activation of the enzyme(s) by NaCl was not observed.

    Original languageEnglish
    Pages (from-to)1443-1446
    Number of pages4
    JournalJournal of biochemistry
    Volume80
    Issue number6
    DOIs
    Publication statusPublished - 1976 Dec

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology

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