Follow-ups of 39 children aged 3 to 12 years who had various biomedical risk factors of local forms of primary tuberculosis. Difficulties in diagnosing the local clinical forms of primary tuberculosis with minor clinical and X-ray signs are shown. The authors show it necessary to use of a package of clinical, laboratory, and radiation techniques, by applying computed tomography.
View Article and Find Full Text PDFUsing 4-methylumbelliferyl (MUF) beta-D-cellobioside as a substrate, the ability of cellobiohydrolase I from Trichoderma longibrachiatum to catalyze transglycosylation has been demonstrated. At substrate concentrations greater than 2 mM, the formation of MUF-tetrasaccharide was detected using HPLC. In the course of enzymatic reaction, a concentration of the transglycosylation product passed through a maximum, since at later stages of the reaction the product was further hydrolyzed.
View Article and Find Full Text PDFThe assay of endo-1,4-beta-glucanases (cellulases) from Trichoderma reesei, T. longibrachiatum, and Sporotrichum pulverulentum by 5-bromoindoxyl-beta-D-cellobioside is described. The substrate is enzymatically cleaved to afford 5-bromoindoxyl and latter undergoes immediate azo coupling with Fast Red or oxidation by nitroblue monotetrazolium chloride, various forms of endoglucanases which can thus be assayed in polyacrylamide gel.
View Article and Find Full Text PDFA very simple and sensitive procedure for the determination of the activity of highly purified endo-1,4-beta-glucanase from the microscopic fungus Trichoderma reesei using 4-methylumbelliferyl-beta-D-cellobioside has been developed. The HPLC study has shown that this substrate is cleaved by endo-1,4-beta-glucanase to form predominantly free 4-methylumbelliferone, Km and kcat being 1.25 mM and 7.
View Article and Find Full Text PDFMicellar solutions of surfactant in organic solvents with rubber additions are proposed for determination of active enzyme concentration. A kinetic theory of enzymatic reactions in reversed micellar systems is developed, suggesting the intermicellar transport of the substrate to be the limiting step in viscous medium. Under these conditions, it is shown that fraction of the product formed after quick transformation of the substrate located in the enzyme-containing micelles depends upon active enzyme concentration and aggregation number of surfactant molecules.
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