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      Permanent link:
      https://www.ias.ac.in/article/fulltext/jbsc/001/03/0295-0304

    • Keywords

       

      Lactic dehydrogenase; Lactobacillus casei ; structure-function; regulation

    • Abstract

       

      Lactic dehydrogenase fromLactobacillus casei ATCC 7469 has been purified to homogeneity by a two-step affinity chromatography procedure which gave an yield of 35%. The enzyme specifically catalysed the conversion of pyruvate to lactate. The enzyme was maximally active at pH 4.6, which was shifted to 5.4 in the presence of fructose 1,6-biphosphate. The enzyme had a molecular weight of 70,800 with two identical subunits, unlike the lactic dehydrogenase from other sources. Histidine and primary amino groups appeared to be involved in catalysis.

    • Author Affiliations

       

      Vanita A Padgaonkar1 S F D’souza1 G B Nadkarni1

      1. Biochemistry and Food Technology Division, Bhabha Atomic Research Centre, Bombay - 400 085
    • Dates

       
  • Journal of Biosciences | News

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