STUDIES ON BACTERIAL AMYLASE:IV. ON THE C-TERMINAL REGION OF BACTERIAL AMYLASE

J-STAGE
  • SUGAE KIN-ICHI
    Laboratory of Biochemistry, Faculty of Science, Osaka University

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Description

The C-terminal amino acid of BA (B. subtilus N') was analyzed by hydrazinolysis and by the use of carboxypeptidase. From the results of hydrazinolysis, it was suggested that C-terminus of BA might be glycine. While, a considerable amount of amino acid was released by the action of carboxypeptidase on native bacterial amylase and no decrease of the amylase activity was observed. Amino acids liberated by carboxypeptidase are leucine and/or isoleucine, valine, phenylalanine, alanine, acidic amino acids, tyrosine, threonine, serine, asparagine and glycine.<br> In contrast to the case of hydrazinolysis, it is remarkable that leucine, valine and phenylalanine are liberated in much larger amounts as compared to that of glycine. No clear cut result was obtained about the nature of C-terminal group of BA. However, it might be suggested that C-terminus of BA is not essential for the enzymatic activity.<br> The author wishes to thank Prof. S. Akabori for his helpful advice throughout this work and also to Nagase Ltd. Co. for the gift of bacterial amylase.

Journal

  • J Biochem (Tokyo)

    J Biochem (Tokyo) 48 (3), 397-405, 1960

    The Japanese Biochemical Society

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