Ostrich pancreatic α-amylase: Kinetic properties, amino terminal sequence and subsite structure

Vaughan Oosthuizen, Ryno J. Naudé, Willem Oelofsen, Muramoto Koji, Kamiya Hisao

    Research output: Contribution to journalArticlepeer-review

    4 Citations (Scopus)

    Abstract

    Ostrich pancreatic α-amylase (OPA) was purified to homogeneity in the presence of protease inhibitors by a single-step affinity chromatography technique. The first 53 amino acids of the N-terminus were identified by gas-phase sequencing. From kinetic parameters (kcat/Km) a subsite profile was established leading to a five subsite model for OPA. The pKa values of catalytic residues were determined as 5.75 and 8.36. Inhibition of OPA by monosaccharides, β-cyclodextrin and a wheat α-amylase inhibitor was studied.

    Original languageEnglish
    Pages (from-to)1313-1321
    Number of pages9
    JournalInternational Journal of Biochemistry
    Volume26
    Issue number10-11
    DOIs
    Publication statusPublished - 1994 Jan 1

    Keywords

    • Ostrich Pancreas α-Amylase N-terminal sequence Subsite profile

    ASJC Scopus subject areas

    • Biochemistry

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