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. 1964 Nov;88(5):1288–1295. doi: 10.1128/jb.88.5.1288-1295.1964

PURIFICATION AND PROPERTIES OF N-ACETYL-d-GLUCOSAMINE KINASE FROM STREPTOCOCCUS PYOGENES

L D Zeleznick a,1, H Hankin a, J J Boltralik a, H Heymann a, S S Barkulis a
PMCID: PMC277406  PMID: 14234783

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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