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Distribution, purification and properties of 1-aspartamido-β-N-acetylglucosamine amidohydrolase

Authors :
I. Strachan
J. Conchie
Source :
Biochemical Journal. 115:709-715
Publication Year :
1969
Publisher :
Portland Press Ltd., 1969.

Abstract

1. The activity of the enzyme that splits 2-acetamido-1-l-β-aspartamido-1,2-dideoxy-β-d- glucose (1-aspartamido-β-N-acetylglucosamine) was measured in tissues from different mammalian species. 2. The enzyme from an aqueous extract of rat liver was purified 150-fold in 56% yield. 3. Optimum activity for the hydrolysis of 1-aspartamido-β-N-acetylglucosamine was at pH7, and ammonia and N-acetylglucosamine were liberated in equimolar amounts. At pH8·5, 1-amino-N-acetylglucosamine was the only sugar produced after short periods of incubation. On prolonged incubation there was spontaneous liberation of ammonia from this compound. 4. It is concluded that the enzyme is an amidase.

Details

ISSN :
03063283
Volume :
115
Database :
OpenAIRE
Journal :
Biochemical Journal
Accession number :
edsair.doi.dedup.....04ce4045f88c54ada53ef99a603f362a
Full Text :
https://doi.org/10.1042/bj1150709