Characterisation of lactic dehydrogenase from Lactobacillus casei.
J Biosci
;
1979 Sept; 1(3): 295-305
Article
in English
| IMSEAR
| ID: sea-160009
ABSTRACT
Lactic dehydrogenase from Lactobacillus 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.
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Index:
IMSEAR (South-East Asia)
Language:
English
Journal:
J Biosci
Year:
1979
Type:
Article
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