A method for the measurement of endo-P-1,3-glucanase is described which combines the simplicity of a reductiometric method with the specificity of a viscometric method. 257
A new method for the detection and assay of α-1,3-glucanases
✍ Scribed by Burton L. Lamberts; Lloyd G. Simonson; Ernest D. Pederson; Robert W. Gaugler
- Publisher
- Elsevier Science
- Year
- 1981
- Tongue
- English
- Weight
- 633 KB
- Volume
- 117
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
✦ Synopsis
A calorimetric method that is specific for the assay of a-1,3-glucanases is presented. The enzyme substrate consists of Cibacron Blue F3GA complexed with a dextranase-treated streptococcal glucan. The method is especially convenient for tests involving large numbers of samples, and can be adapted to quantitative as well as qualitative applications. The assay is sufficiently sensitive for screening bacterial samples as potential sources of a-1,3-glucanase.
📜 SIMILAR VOLUMES
New soluble chromogenic substrates were prepared for specific and rapid assays of endo-l,4-/3-xylanases and endo-1 ,4+glucanases. A soluble beechwood 4-0-methyl-D-glucurono-D-xylan was dyed with Remazol brilliant blue R, and hydroxyethylcellulos was coupled to Ostazin brilliant red H-3B. The assays
We have developed an improved assay method to measure sphingomyelinase activity and to detect this enzyme separated on polyacrylamide gels. The assay of sphingomyelinase activity involved immobilizing \(\left[\mathbf{N}\right.\)-methyl \(\left.{ }^{14} \mathrm{C}\right]\) sphingomyelin on polyvinyld