Studies on glucosaminidase. 2. Substrates for N-acetyl-β-glucosaminidase*
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چکیده
منابع مشابه
Studies on glucosaminidase. 2. Substrates for N-acetyl-beta-glucosaminidase.
the oxygen uptake and acetoacetate oxidation when added alone or with fumarate, but not in the presence of a-oxoglutarate. The reasons for these differences are discussed. Anaerobically, relatively slight inhibitions of the reduction of acetoacetate were observed. 6. The oxidation of L( + )-p-hydroxybutyrate is inhibited by dinitrophenol, whereas that of the D(-)-form is not. This is related to...
متن کاملUrinary biomarker N-acetyl-β-D-glucosaminidase can predict severity of renal damage in diabetic nephropathy
BACKGROUND Diabetic nephropathy is a clinical diagnosis where proteinuria is present in a patient with diabetes. Early intervention can significantly improve the prognosis. However, imprecision of the currently available biomarkers have impaired effective therapies in a timely manner. Urinary N-acetyl-β-D-glucosaminidase (NAG) is excreted in abnormally high amounts in many renal diseases. The a...
متن کاملDown-regulation of β-N-acetyl-D-glucosaminidase increases Akt1 activity in thyroid anaplastic cancer cells.
O-GlcNAcylation is a common and dynamic modification of intracellular proteins in which β-N-acetyl-glucosamine moieties are attached to hydroxyl groups of serine or threonine residues (O-GlcNAc). Accumulating evidence suggests the critical role of protein O-GlcNAcylation in signal transduction, transcriptional control, cell cycle regulation and protein degradation. However, the exact role of O-...
متن کاملSpectrophotometricAssayfor UrinaryN-Acetyl-f3-D-Glucosaminidase Activity
An improved assay for N-acetyl-/3-o-glucosaminidase activity in urine is described that involves (a) gel filtration to separate the enzyme from inhibitors in urine, (b) enzymic hydrolysis of p-nitrophenyl-N-acetyl-3-D-glucosaminide at pH 4.4, and (C) spectrophotometry of the liberated p-nitrophenylate. Measurements of activity of the enzyme in 58 urine specimens correlated closely (r = 0.9998) ...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1961
ISSN: 0306-3283
DOI: 10.1042/bj0780106