Related Experiment Video
Updated: Sep 3, 2026

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
Published on: December 9, 2017
PURIFICATION AND PROPERTIES OF N-ACETYL-D-GLUCOSAMINE KINASE FROM STREPTOCOCCUS PYOGENES
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.
More Related Videos
11:06GC-based Detection of Aldononitrile Acetate Derivatized Glucosamine and Muramic Acid for Microbial Residue Determination in Soil
Published on: May 19, 2012
13:53Homogeneous Glycoconjugate Produced by Combined Unnatural Amino Acid Incorporation and Click-Chemistry for Vaccine Purposes
Published on: December 19, 2020
Related Concept Videos
Biosynthesis of Polysaccharides
Protein Folding Quality Check in the RER
Oligosaccharide Assembly
Multiple sugar molecules that may or may...
Glycosaminoglycans
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...