Ostrich (Struthio camelus) carboxypeptidase A: Purification, kinetic properties and characterization of the pancreatic enzyme

Graeme Bradley, Ryno J. Naude, Koji Muramoto, Fumio Yamauchi, Willem Oelofsen

    Research output: Contribution to journalArticlepeer-review

    10 Citations (Scopus)

    Abstract

    1. 1. Carboxypeptidase A and carboxypeptidase A,-type from the pancreas of the ostrich were purified by water extraction of acetone powder, aminobenzylsuccinic acid affinity and hydroxylapatite chromatography. 2. 2. The final preparations were homogeneous when subjected to SDS-PAGE and PAGE. The M, values obtained from SDS-PAGE for CPAp and CPA,-type were 34,600 and 34,400, respectively. 3. 3. The effects of inhibitors (1,10 phenanthroline and indole-3-acetic acid), pH and temperature on CPA activity were examined. Ki-values for CPI, PPA, D-phe, D-trp and aminobenzylsuccinic acid were determined. 4. 4. Km, kcat and kcat/Km values were determined for hipp-phe, cbz-gly-phe, cbz-(gly)2-phe, cbz-gly-leu, cbz-(gly)2-leu and cbz-(gly)2-val. 5. 5. N-terminal sequencing and amino acid analysis were performed for CPAβ and CPAτ-type.

    Original languageEnglish
    Pages (from-to)555-564
    Number of pages10
    JournalInternational Journal of Biochemistry
    Volume26
    Issue number4
    DOIs
    Publication statusPublished - 1994 Apr

    ASJC Scopus subject areas

    • Biochemistry

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