We describe a simple endpoint method for the determination ofN-acetyl-@ghtcosaminidase (NAGase; EC 3.2.1.30). NAGase uses a fluorogenic substrate, 4-methylumbelliferyl-IV-acetyl-@tx-ghtcosaminide, at pH 4.6, liberating the fluorescent 4-methylumbelliferone. The method is reproducible and fast both a
A convenient assay for chitinase that uses partially N-acetylated chitosans as substrates
β Scribed by Sei-ichi Aiba
- Publisher
- Elsevier Science
- Year
- 1992
- Tongue
- English
- Weight
- 242 KB
- Volume
- 230
- Category
- Article
- ISSN
- 0008-6215
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## N-Acetyl-L-phenylalanyl-L-34hiaphenylalanine has been shown to be a substrate for carboxypeptidase A. Hydrolysis of the compound obeys Michaelis-Menten kinetics with a KM of 0.22 mM and a k,,, of 6720 min-' at 22Β°C. A calorimetric assay, employing Ellman's reagent to detect the thiophenol relea
N,N',N"-Tri(monochloro)acetylchitotriose prepared by N-monochloroacetylation of chitotriose trihydrochloride was successfully polymerized into higher-molecular-weight oligomers by a lysozyme-catalyzed transglycosylation reaction, and a following base-catalyzed N-demonochloroacetylation gave a chitos
Currently, protein phosphatase 2B (calcineurin) activity is assayed based on release of [32P]phosphate from a 19-amino acid peptide (partial sequence of the regulatory subunit of cAMP-dependent protein kinase) following its [32P]ATP phosphorylation using the catalytic subunit of cAMP-dependent prote