Most of the methods currently available for the determination of RNase activity are dependent on the measurement of acid-soluble products released 'by hydrolysis of RNA. The major advantages of these methods are that they are sensitive, reproducible, and convenient for large numbers of samples (l-3)
Accurate assay of low intestinal lactase activity with a fluorometric method
β Scribed by Arne Dahlqvist; Nils-Georg Asp
- Publisher
- Elsevier Science
- Year
- 1971
- Tongue
- English
- Weight
- 201 KB
- Volume
- 44
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
β¦ Synopsis
Assay of small-intestinal lactase activity in jejunal biopsies is usually performed with the Tris/glucose oxidase reagent of Dahlqvist
(1,2) or more or less modified methods. The glucose oxidase methods are simple and well suited for differentiation of the low activities in lactase-deficient individuals from the high activities in individuals with persistent lactase.
Accurate assay and characterization of the low residual lactase activity in lactase deficient individuals is of interest for the understanding of the biochemical alteration and genetic mechanism of different forms of human lactase deficiency. The high concentration of mucosal homogenate needed for assay of very low activities, however, tends to interfere with the glucose oxidase-peroxidase system (3)) making internal standards necessary.
The galactose dehydrogenase-NAD+ method now reported has the advantage of being five times more sensitive than the ultramioromodification (2) of the glucose oxidase method. The system is also not influenced even by high concentrations of mucosal homogenate in the incubation mixture. MATERIALS
π SIMILAR VOLUMES
The activity of peptidylarginine deiminase (PAD) has generally been assayed by a colorimetric method using N-benzoyl-L-arginine ethyl ester (BAEE) and Nbenzoyl-L-arginine (Bz-L-Arg) as the substrates. The widespread occurrence of citrulline and urea in tissues makes use of this method difficult, esp
A rapid and sensitive method is described for determining the activity of alanine racemase (5. I. I. I) with its substrates. Alanine racemase from Bacillus subtilis catalyzes the exchange of the (Y hydrogen of L and D alanine, a racemic mixture of alanine as we!! as both the Q hydrogens of glycine w