Direct and continuous spectrophotometric assay of β-glucosidase
✍ Scribed by B.H.J. Hofstee
- Book ID
- 118840866
- Publisher
- Elsevier Science
- Year
- 1955
- Tongue
- English
- Weight
- 391 KB
- Volume
- 59
- Category
- Article
- ISSN
- 0003-9861
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The neutral pH optimum beta-glucosidases of mammalian liver and almonds are each capable of hydrolyzing a number of plant glucosides, including L-picein (p-hydroxyacetophenone-beta-D-glucoside) and prunasin (D-mandelonitrile-beta-D-glucoside). Taking advantage of the marked differences in the spectr
Herein we report the development of a direct and continuous spectrophotometric method for determining transglutaminase (TGase) activity by using N,Ndimethyl-1,4-phenylenediamine (DMPDA) as a ␥-glutamyl acceptor substrate and carbobenzyloxy-Lglutamylglycine (Z-Gln-Gly) as a typical peptide ␥-glutamyl