Open AccessPurification and Properties of N ‐Acetylglucosamine Kinase from Human Gastric Mucosa
Author(s) -
GindzieŃSKI Andrzej,
Glowacka Danuta,
Zwiez Krysztof
Publication year - 1974
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1974.tb03395.x
Subject(s) - n acetylglucosamine , enzyme , aminosugar , biochemistry , chemistry , acetylglucosamine , gastric mucosa , kinase , phosphorylation , glucosamine , stomach
N ‐Acetylglucosamine kinase from the human gastric mucous membrane was purified about 170‐fold. The purified enzyme is specific for N ‐acetylglucosamine with slight phosphorylation of N ‐acetylmannosamine. The aminosugar product of the enzymatic reaction was identified as N ‐acetylglucosamine 6‐phosphate. The Km for N ‐acetylglucosamine is 0.11 K m and for ATP 3.03 mM. The pded enzyme is stable at +4 °C for three days, labile to dialysis and irreversibly inhibited by p ‐chloromercuribenzoate. The molecular weight of the enzyme was 77000.