PURIFICATION AND PROPERTIES OF N-ACETYL-d-GLUCOSAMINE KINASE FROM STREPTOCOCCUS PYOGENES
AUTOR(ES)
Zeleznick, L. D.
RESUMO
Zeleznick, L. D. (CIBA Pharmaceutical Co., Summit, N.J.), H. Hankin, J. J. Boltralik, H. Heymann, and S. S. Barkulis. Purification and properties of N-acetyl-d-glucosamine kinase from Streptococcus pyogenes. J. Bacteriol. 88:1288–1295. 1964.—A kinase from Streptococcus pyogenes which catalyzes adenosine triphosphate-dependent phosphorylation of d-glucose and N-acetyl-d-glucosamine has been purified 1,500-fold. The ratio of the enzymatic activity on both substrates remained constant throughout the fractionation. Similarity in heat stability, p-hydroxymercuribenzoate inhibition, protection by either carbohydrate, and lack of repression of enzymatic activity when the bacteria were grown exclusively on one of the two substrates supports the hypothesis that kinase activity is associated with one enzyme.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=277406Documentos Relacionados
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