✦ LIBER ✦

Assay and properties of N-acetylglucosamine-6-phosphate deacetylase from rat liver

✍ Scribed by Patrick Campbell; Torvard C. Laurent; Lennart Rodén

Publisher: Elsevier Science
Year: 1987
Tongue: English
Weight: 622 KB
Volume: 166
Category: Article
ISSN: 0003-2697
DOI: 10.1016/0003-2697(87)90555-0

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✦ Synopsis

A single-vial assay has been developed for N-acetylglucosamine-6-phosphate deacetylase. in which ['HIacetate released from 'H-acetyl-labeled substrate is measured in a biphasic liquid scintillation counting system after acidification of the reaction mixture. The deacetylase was partially purified from rat liver, and some of its properties were determined. Chromatography on a calibrated Sepharose CL.-6B column indicated a molecular weight of 345.000. The K,,,,, for the substrate at pH X.0 was 0.3 mM. Glucosaminc 6-phosphate and glucose h-phosphate inhibited the enzyme, whereas !V-acctylgalactosamine. h'-acetylglucosamine. &'-acetqlglucosamine I-phosphate.

and glucosamine I-phosphate were without effect. The effects of several divalent cations were also examined.

Under the conditions tested. Ca'+, Mg". and Ba'+ had essentially no effect, whereas Mn'+. Ni", and CL?+ were inhibitory and Co'+ stimulated activity at low concentrations but inhibited above 5 mM. An increase in the ionic strength of the reaction mixture to 0.3 M decreased the activity by 40%.

IZ~ 1~87 Academic PESS. inc.

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