A sensitive method for the detection of aspartate: 2-oxoglutarate aminotransferase activity on polyacrylamide gels
โ Scribed by Toshiharu Yagi; Hiroyuki Kagamiyama; Mitsuhiro Nozaki
- Publisher
- Elsevier Science
- Year
- 1981
- Tongue
- English
- Weight
- 813 KB
- Volume
- 110
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
โฆ Synopsis
A sensitive technique for the qualitative and semiquantitative determination of the activity of aspartate aminotransferase on polyacrylamide gels after electrophoresis is described. It relies on the ability of aspartate aminotransferase to produce SOS--in the transamination between L-cysteine sulfinate and 2-oxoglutarate. The method is based on the reduction of nitroblue tetrazolium by SOS--using phenazine methosulfate as a coupling agent. The method has been characterized using human and pig sera, crude homogenates and crystalline preparation from pig heart muscle, and bacterial crude extracts.
๐ SIMILAR VOLUMES
A simple and rapid staining procedure is described for qualitative and quantitative determination of the activity of plant (Citrus sinensis (L.) Osbeck cv. Shamouti) andfungal (Trichodermata viride) cellulases in polyacrylamide gels. The method is based on the incorporation of carboxymethyl cellulos
An optimized method for reverse staining of proteins in polyacrylamide gels is described. The method is based on the selective precipitation of a white imidazole-zinc complex all along the gel except in the protein bands. The high selectivity of this method allows a "toning procedure" which turns th
A method is described for the specific detection of urocanase activity on polyacrylamide gels. It is dependent upon the reduction of nitro blue tetrazohum by the product of the urocanase reaction using phenazine methosulphate as a coupling agent. The method has been characterized using crude cell ex