enzyme produces beta-xylose from beta-xylopyranosides while retaining the anomeric configuration of the xylose in the substrate. Enzyme shows transglycosylation activities in the presence of alcohols as acceptors. No substrate: 4-nitrophenyl-alpha-L-arabinofuranoside, 4-nitrophenyl-alpha-D-xylopyranoside, 4-nitrophenyl-alpha-D-glucopyranoside, and 4-nitrophenyl-beta-D-glucopyranoside, oat spelt xylan, birch wood xylan, or carboxymethyl cellulose
enzyme produces beta-xylose from beta-xylopyranosides while retaining the anomeric configuration of the xylose in the substrate. Enzyme shows transglycosylation activities in the presence of alcohols as acceptors. No substrate: 4-nitrophenyl-alpha-L-arabinofuranoside, 4-nitrophenyl-alpha-D-xylopyranoside, 4-nitrophenyl-alpha-D-glucopyranoside, and 4-nitrophenyl-beta-D-glucopyranoside, oat spelt xylan, birch wood xylan, or carboxymethyl cellulose
Identity of beta-glucosidase, beta-xylosidase and one of the beta-galactosidase activities in human liver when assayed with 4-methylumbelliferyl-beta-D-glycosides studies in cases of Gaucher's disease.
Experiments to increase the selectivity of tumor chemotherapy by means of in vivo activation of transport forms of cancerostatics by exogenous enzymes.
[Distribution studies of alpha-L-arabinofuranosidase already unstable at pH 7.0 (37 degrees C) in tumor-bearing mice in connection with its possible use to enhance the selectivity of the chemotherapy of malignant tumors]
[Experiments on the modification of the distribution of the activity of various alpha-L-arabinofuranosidases following i.v. application in tumor-bearing mice]
with use of vector pHsh, expression of XylC increases approximately 4fold when a loop within the translational initiation region in the mRNA is removed by site-directed mutagenesis. The increased expression of xylCm is due to removal of a stem-loop structure without a change of the amino acid sequence of the heterologously expressed enzyme
with use of vector pHsh, expression of XylC increases approximately 4fold when a loop within the translational initiation region in the mRNA is removed by site-directed mutagenesis. The increased expression of xylCm is due to removal of a stem-loop structure without a change of the amino acid sequence of the heterologously expressed enzyme