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Distribution, purification and properties of 1-aspartamido-β-N-acetylglucosamine amidohydrolase
- 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.
- Subjects :
- Male
History
Swine
Guinea Pigs
Kidney
Amidohydrolases
Education
Amidase
Mice
chemistry.chemical_compound
Hydrolysis
Ammonia
Testis
N-Acetylglucosamine
Animals
Humans
Sugar
Incubation
Epididymis
chemistry.chemical_classification
Chromatography
Glucosamine
Sheep
Amidohydrolase
Deer
Brain
Articles
Hydrogen-Ion Concentration
Plants
Rats
Computer Science Applications
Enzyme
Liver
chemistry
Biochemistry
Mollusca
Liberation
Cattle
Spleen
Subjects
Details
- ISSN :
- 03063283
- Volume :
- 115
- Database :
- OpenAIRE
- Journal :
- Biochemical Journal
- Accession number :
- edsair.doi.dedup.....04ce4045f88c54ada53ef99a603f362a
- Full Text :
- https://doi.org/10.1042/bj1150709