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At least 649 records · Page 36Linked to original sources
PubMed2001

Promotive effect of auxins on UDP-glucose: flavonol glucosyltransferase activity in Vitis sp. cell cultures.

The addition of 2,4-dichlorophenoxyacetic acid (2, 4-D) to Vitis sp. cell cultures significantly enhanced the production of quercetin 3,7,4'-tri-O-glucoside, 3,7-di-O-glucoside and 3,4'-O-glucoside from quercetin. This enhancement of glucosylation by 2,4-D was also observed in cell cultures of other plant species. The activity of UDP-glucose: flavonol glucosyltransferase (UFGT) in cell-free extracts of Vitis sp. cell cultures increased approximately 10-fold, 48 h after the addition of 2,4-D to the culture medium. The UFGT activity increased linearly up to 15 h and showed a maximal response to the addition of 10-50 mg/l of 2,4-D at 48 h. The promotive effect of 2,4-D was inhibited by cycloheximide suggesting that de novo protein synthesis was involved in this phenomenon. Interestingly, similar promotive effects on the UFGT activity were observed for other phytohormones such as kinetin and several anti-auxins.

Journal Article↗
PubMed2001

Functional glucosylation of kojic acid and daidzein with the Eucalyptus membrane-associated UDP-glucosyltransferase reaction system.

Kojic acid was glucosylated to kojic acid 5- and 7-O-beta-D-glucopyranosides by cultured cells of Eucalyptus perriniana. The glucosylation was also performed effectively by the enzymatic reaction system using membrane-associated UDP-glucosyltransferase from the cells with addition of UDP-glucose. The production of the 5-O-D-glucoside occurred exclusively prior to that of the 7-O-glucoside in both systems. In the same manner, daidzein was converted to daidzin (daidzein 7-O-beta-D-glucopyranoside) by the enzymatic system. Here, we propose methods for the structural modification of phytoestrogen-related substances by enzymatic beta-glucosylation.

Journal Article↗
PubMed1990

[Initial-plaque forming ability of glucosyltransferases from Streptococcus mutans serotype C strain].

In order to clarify functional roles of extracellular glucosyltransferases (GTases) from S. mutans serotype c in initial stage of plaque formation, GTase-I and GTase-S were purified from culture fluids of strain PS 14. And an ability of these GTases to enhance cellular attachment of oral streptococci was investigated using 3H labeled resting cells of S. sanguis Challis and S. milleri Is 57. The results were as follows: 1) From culture fluids of strain PS 14 grown in a M 4 medium supplemented with 1% ammonium sulfate, GTase-I was purified by ammonium sulfate fractionation, CM-cellurose column chromatography and Toyopearl HW-55 gelfiltration. Also, GTase-S was purified by the method of Baba et al from the culture fluids of strain PS 14 grown in a dialyzed BHI medium. Purified GTase-I and GTase-S were almost homogeneous, and had a molecular size of 160 KDa and 145 KDa respectively (by SDS-PAGE). 2) Sucrose-dependent attachment of S. sanguis cells to experimental pellicles was markedly enhanced by the addition of crude GTase in saliva. This fact was conformed by a scanning electron microscopic observation of the attachment cells. Such enhanced attachment necessitated a long-term incubation (greater than 10 h) of the cells in the presence of sucrose, suggesting that it is correlated to de novo glucan synthesis. 3) Purified GTase-I also had an ability to enhance the cellular attachment of S. sanguis cells as well as crude GTase, while purified GTase-S didn't have. Neither crude enzyme, GTase-I nor GTase-S have an ability to enhance significantly the cellular attachment of S. milleri cells. However, S. milleri pretreated with the preparations containing GTase-S gained the ability to attach to experimental pellicles prepared from saliva supplemented with GTase-I. These results suggest that the cellular attachment system mediated by enzymatic action (s) of GTase (s) from serotype c S. mutans be present and function in the first stage of plaque formation.

Cell Adhesion↗
PubMed1994

Plant biochemistry of xenobiotics: isolation and characterization of a soybean O-glucosyltransferase of DDT metabolism.

The insecticide DDT is metabolized in soybean and wheat cell cultures to the acylglucoside of 2,2-bis-(4-chlorophenyl)-acetic acid (DDA) (M. Arjmand and H. Sandermann, 1985, Pesticide Biochem. Physiol. 23, 389-397). An enzyme catalyzing the conjugation reaction has been highly purified from the soluble enzyme fraction of cultured soybean cells. After the initial ammonium sulfate fractionation, quercetin and pentachlorophenol were preferentially glucosylated. In the course of 367-fold purification, DDA became the preferred substrate. The purified enzyme was unstable. A molecular weight of approximately 50 kDa was estimated for the native enzyme (gel permeation chromatography) as well as the denatured protein (sodium dodecyl sulfate-gel electrophoresis). The isoelectric point for the enzyme was near pH 4.9. Apparent Km values of about 170 microM were determined for UDP-glucose as well as DDA. The maximal velocity was 257 microkat/kg protein, corresponding to a conjugation capacity of 855 micrograms DDA/h/g fresh weight of cells.

Chromatography, Affinity↗
PubMed1978

Antibodies against Streptococcus mutans and glucosyltransferases in caries-free and caries-active military recruits.

1) Plaque samples from caries-active recruits showed a higher incidence of S. mutans than plaque samples from caries-free recruits. The persistance of the S. mutans serotypes in the individual plaque samples attested to the consistency of S. mutans in human dental plaque. 2) S. mutans serotype d is predominantly present in approximal plaque of caries-active subjects. 3) Serum antibody titers against S. mutans are higher in caries-active individuals. 4) Sera from caries-free or caries-active individuals inhibit the insoluble glucan synthesis by the cellbound GTF to the same extent. 5) It is unlikely that antibodies against S. mutans in parotid saliva or serum play a major role in the protection against dental caries in Dutch military recruits.

Adult↗
PubMed1978

Interaction of Streptococcus mutans glucosyltransferases with antibodies.

1) The GTF-A and GTF-B activities of serotype (c), (e), and (f) organisms are antigenically more closely related to each other than to the comparable enzymes from organisms of the other four S. mutans serotypes. 2) The adherence-inhibiting antibody in anti-GTF-A appears to be mediated against a heat sensitive cell surface antigen of S. mutans - most likely GTF activity. However, unequivocal proof of this conclusion awaits the preparations of homogeneous GTF-A preparations.

Adhesiveness↗