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At least 19 recordsLinked to original sources
PubMed1977

The absorption of protons with alpha-methyl glucoside and alpha-thioethyl glucoside by the yeast N.C.Y.C. 240. Evidence against the phosphorylation hypothesis.

1. When yeast N.C.Y.C. 240 was grown with maltose in a complex medium based on yeast extract and peptone, washed cell preparations fermented alpha-methyl glucoside much more slowly than maltose. 2. The yeast absorbed alpha-methyl[14C]glucoside from a 10mM solution in the presence of antimycin and iodoacetamide, producing [14C]glucose, which accumulated outside the cells. The yeast itself contained hexose phosphates, trehalose, alpha-methyl glucoside and other products labelled with 14C, but no alpha-methyl glucoside phosphate. 3. About 1 equiv. of protons was absorbed with each equivalent of alpha-methylglucoside, and 1 equiv. of K+ ions left the yeast. 4. alpha-Thioethyl glucoside was also absorbed along with protons. Studies by g.l.c. showed that the yeast concentrated the compound without metabolizing it. 5. The presence of trehalose, sucrose, maltose, L-sorbose, glucose or alpha-phenyl glucoside in each case immediately stimulated proton uptake, whereas fructose, 3-O-methylglucose and 2-deoxyglucose failed to do so. 6. The observations support the conclusion that alpha-thioethyl glucoside, alpha-methyl glucoside and maltose are substrates of one or more proton symports, whereas they seem inconsistent with the notion that the absorption of alpha-methyl glucoside involves the phosphorylation of the carbohydrate [Van Stevenick (1970) Biochim. Biophys. Acta 203, 376-384].

Carbohydrate Metabolism↗
PubMed1975

Biosynthesis and structure of glycosyl diglycerides, steryl glucosides, and acylated steryl glucosides.

A particulate enzyme fraction from Mycobacterim smegmatis catalyzed the transfer of -14C-glucose from the UDP--14C-glucose into neutral glycolipids. The two major radioactive components were purified by column chromatography on O-diethylamino ethyl cellulose (acetate) and thin layer chromatography on silica gel in several solvents. The first product yielded a water-soluble component upon saponification, which had a hexoseglycerol ratio of 1:1 with all of the hexose being identified as glucose. The second product yielded a water-soluble component upon saponification which contained hexose and glycerol in a 2:1 ratio and, in addition to glucose, contained lesser amounts of mannose and galactose. Palmitate and oleate were the predominant fatty acids and were present in equimolar amounts. The products thus have been identified as monoglycosyldiglyceride and diglycosyldiglyceride. The diglycosyldiglyceride could also be labeled with -14C-galactose when UDP--14C-galactose served as the donor, but the monoglycosyldiglyceride was only slightly labeled with -14C-galactose. Membrane fractions from mung bean seedlings catalyzed the transfer of -14C-glucose from UDP--14C-glucose into a neutral glycolipid which has been purified by thin layer chromatography and analyzed by combined gas liquid chromatography-mass spectrometry. It was determined to be a steryl glucoside with the two major sterol components being betasitosterol and stigmasterol linked to beta-D-glucose. Particulate fractions from developing cotton fibers also catalyzed the formation of steryl glucosides and, in addition, they catalyzed the esterification of steryl glucosides at the 6 position of glucose with fatty acids (primarily palmitate and oleate) from an andogenous acyl donor. Both the glucosyl transferase and the acyltransferase have been solubilized with Triton X-100 and partially purified by chromatography on Sephadex G-200. The acyltransferase activity was reconstituted by the addition of the steryl glucoside and a phospholipid acyl donor.

Acyltransferases↗
PubMed1979

The use of octyl beta-D-glucoside as detergent for hog kidney brush border membrane.

Octyl beta-D-glucoside was synthetized from alpha-acetobromoglucose with an improved method yielding a very pure product with a sharp melting point (108-109 degrees C) and free of intermediate products as judged by IR and NMR spectra. The yield of the synthesis is 66% when referred to alpha-acetobromoglucose. The potency of this compound as a detergent on hog kidney brush border membranes was compared to the action of Triton X-100. Octyl glucoside preferentially extracts aminopeptidase M and gamma-glutamyltranspeptidase in a concentration-dependent manner. The more deeply imbedded membrane enzyme, alkaline phosphatase, was relatively resistent to the action of octyl glucoside. In contrast, Triton X-100 extracted all membrane proteins to about the same extent. Additionally it was found that octyl glucoside can be removed from membrane extracts by Biobead SM 2. The capacity of the beads is about 170 mg detergent/g of dry Biobead SM 2. Thus octyl glucoside seems to be a useful tool for solubilization and purification of brush border membranes proteins.

Animals↗
PubMed1979

Unmasking of an essential thiol during function of the membrane-bound enzyme II of the phosphenolpyruvate beta-glucoside phosphotransferase system of Escherichia coli.

beta-Glucoside transport by phosphoenolpyruvate-hexose phosphotransferase system in Escherichia coli is inactivated in vivo by thiol reagents. This inactivation is strongly enhanced by the presence of transported substrates. In a system reconstituted from soluble and membrane-bound components, only the particulate component, the membrane-bound enzyme IIbgl appeared as the target of N-ethylmaleimide inaction. The same feature was found in the case of methyl-alpha-D-glucoside uptake via enzyme IIglc. It is shown that the sensitizing effect of substrates is specific and not generalized, methyl-alpha-D-glucoside only sensitizes enzyme IIglc and p-nitrophenyl-beta-D-glucoside only sensitizes enzyme IIbgl towards N-ethylmaleimide inactivation. The inactivation of enzyme IIbgl by thiol reagents is also promoted in vivo by fluoride inhibition of phosphoenolpyruvate synthesis. In toluene-treated bacteria, the presence of phosphoenolpyruvate protects against inactivation by thiol reagents of p-nitrophenyl-beta-D-glucoside phosphorylation. Both results suggest that the inactivator resistent form of enzyme IIbgl is an energized form of the enzyme.

Chloromercuribenzoates↗
PubMed1977

Antitumour and immunosuppressive activity of hydroxyanthraquinones and their glucosides.

Both isomeric monohydroxyanthraquinones (1a, b), three dihydroxyanthraquinones (alizarin 1c, chrysazin 1d, and anthraflavin 1e) and corresponding acetylated (2) and free (3) beta-D-glucosides were screened for antitumour and immunosuppressive activity. Furthermore, four O-acetyl and O-benzyl derivatives of alizarin (5a--d) were tested. Antitumour activity was judged by the inhibition of growth of syngeneic tumours in the treated recipients and immunosuppressive activity by the effect on tumour growth or on skin graft survival in pretreated allogeneic recipients; as standard of reference served the activity of certain cancerostatic or immunosuppressive drugs used in clinical practice. 1-Hydroxyanthraquinone (1a), alizarin (1c), chrysazin (1d), acetylated glucoside of 2-hydroxyanthraquinone (2b), 2-benzylalizarin (5c), and 1-acetyl-2-benzylalizarin (5d) were found to exhibit antitumour activity. Distinct immunosuppressive activity was detected in alizarin (1c), acetylated glucoside of 1-hydroxyanthraquinone (2a), acetylated glucoside of 2-hydroxyanthraquinone (2b), acetylated glucoside of chrysazin (2d), 2-acetylalizarin (5a), and 1-acetyl-2-benzylalizarin (5d). The group of hydroxyanthraquinone glucodises (3a--3d) exhibited neither antitumour nor immunosuppressive activity.

Animals↗
PubMed1975

Beta-Glucosidases from Cicer arietinum L. Purification and Properties of isoflavone-7-O-glucoside-specific beta-glucosidases.

Beta-Glucosidases specific for isoflavone 7-O-glucosides have been isolated from garbanzo plants, Cicer arietinum L. These aryl-beta-glucohydrolases occur in the different organs of the plant as multiple molecular forms. The major isoenzymes of the roots, the leaves and the hypocotyl were purified to electrophoretic homogeneity. When subjected to isoelectric focussing in polyac rylamide gels the electrophoretically homogeneous glucohydrolases were found to consist of one or two major and several minor enzymically active molecular species. In roots the beta-glucohydrolase isoenzymes constitute a considerable portion of the extractable protein, so that purification to an electrophoretically homogeneous form is easily attainable. All beta-glucosidases analyzed possess molecular weights in the range of 125 000 (ultracentrifugation) to 135 000 (Sephadex G-200) and contain two subunits of molecular weight near 68 000. The pH optimum for enzymic activity is 7--7.5 with a second optimum of 4.5--5. The isoelectric points of the various species range between pH 5.9 AND 7.1. Staining for glycoprotein was positive. Kinetic analysis demonstrated a pronounced specificity of the enzymes for aromatic substrates with glucose as the sugar moiety. alpha-Glucosides as well as disaccharides were not hydrolyzed at all. Isoflavone 7-O-glucosides are the most favoured substrates with a Km of 2 x 10(-5) M, while the Km with aromatic glucosides (i.e. salicin, 4-nitrophenyl glucoside) are 100 times larger. In addition the beta-glucosidases show a pronounced specificity for glucose in the 7-position of the flavonoid nucleus. Using isoflavone aglycones as substrates glucose transferase activity was also demonstrable. The beta-glucohydrolase activity is strongly inhibited by Hg2plus. This inhibition is partially reversible and preferentially influences the Km values of the enzymes compared to V. Agplus, glucono-1,5-lactone, ethyleneglycol monomethyl ether and glycerol are only weakly inhibitory, while glucose, p-chloromercuribenzoate and Cu2plus are without effect.

Flavonoids↗
PubMed1976

[Histochemical and biochemical investigation of alpha-glucosidases by means of 2-naphthyl-alpha-D-glucoside (author's transl)].

Histochemical and biochemical studies yield the following method of choice for the in situ detection of neutral (microvillous) and acid (lysosomal) alpha-glucosidases: 12 mg 2-naphthyl-alpha-D-glucoside (dissolved in 0.5 ml N,N-dimethylformamide) and 0.6--0.8 ml hexazonium-p-rosaniline in 10 ml 0.1 M citric acid phosphate buffer for aqueous or 5 ml buffer mixed with equal parts of 2% agar for incubation with semipermeable membranes, pH 5 or 6.5. With this method neutral alpha-glucosidases can be exactly demonstrated in the brush border of the small intestine (glycoamylase, sucrase-isomaltase) and kidney of mammals, birds,fishes, amphibia and reptiles; localization of acid alpha-glucosidases is achieved at the cellular level in many organs and tissues. Fluorometric and photometric measurements prove that 2-naphthyl-alpha-D-glucoside is superior to 6-brom-2-naphthyl-alpha-D-glucoside for the demonstration of alpha-glucosidases in situ due to the lower Michaelis constant and higher maximal reaction velocity of the naphthol derivative.--Among the coupling reagents tested neutral alpha-glucosidases can be localized correctly with hexazotized p-rosaniline (with and without semipermeable membranes) for simultaneous coupling. Fast Blue B delivers false positive results in the suczedaneous and simultaneous coupling procedure using aqueous incubation media; in combination with the membrane technique azo dye can not be observed in the sections. Hexazonium-p-rosaniline inhibits neutral and acid alpha-glucosidases to nearly the same extent as Fast Blue B. Fixation of blocks of tissue in formaldehyde and glutaraldehyde suppresses alpha-glucosidases in the intestine and epididymis. The inhibition rates amount to 50 and 70% respectively. Washing in sugar solution rises enzyme activity to 65 and 50%. Species and organ dependent activity differences of neutral and acid alpha-glucosidases and changes of enzyme activity in the intestine and kidney after castration as well as in the course of pregnancy can be detected by means of biochemistry but not with the histochemical assay including minimal incubation. In comparison with p-nitrophenyl-alpha-D-glucoside the 2-naphthyl derivative is also the substrate of choice for the biochemical determination of alpha-glucosidases.--Agar gel electrophoresis reveals one band in the neutral and acid pH range.

Animals↗
PubMed1979

[Interrelationship between glucoside-bound and free alcohols during ether oil formation in rose petals].

Some data on the dynamics of free and glucoside-bound monoterpenic and aromatic (beta-phenylethyl) ethers content and the changes in the beta-glucosidase activity in rose petals at different stages of the flower development and on the kinetics of enzymatic hydrolysis of these glucosides are presented. The phase specificity of beta-glucosidase coinciding with the maximal accumulation of glucoside-bound and free alcohols is revealed. The data obtained suggest that the formation of glucosides may precede the accumulation of corresponding free alcohols of terpenic and aromatic origin.

Alcohols↗
PubMed1978

Chemical constituents of gentianaceae XXIII: tetraoxygenated and pentaoxygenated xanthones and xanthone O-glucosides of Swertia angustifolia Buch.-Ham.

The whole plant extract of Swertia angustifolia Buch.-Ham., collected at different stages of growth, contained 14 tetraoxygenated and five pentaoxygenated xanthones and xanthone 1-O-glucosides. Of the eight xanthone 1-O-glucosides isolated, five were previously unreported in nature. The xanthones are broadly based on 1,3,5,8- and 1,3,7,8-oxygenated systems, with an added oxygen function at C-4 in some compounds, and represent a number of methoxylated patterns. The content and relative abundance of the free xanthones and their 1-O-glucosides changed with plant growth. These results are the first demonstration of the variation in chemical characters in the different parts of a Swertia species during its ontogeny. The biolgocial significance of these results is appraised.

Glucosides↗
PubMed1976

Studies in the design of x-ray contrast agents. Synthesis, hydrophobicity, and solubility of some iodoresorcyl bis(beta-glucosides).

Two diiodo- and two triiodoresorcyl bis(beta-glucosides) were prepared and their hydrophobicity (log P octano) and water solubility were compared to a triiodophenyl beta-glucoside and several experimental nonionic, water-soluble, x-ray contrast agents. The data indicate steric overlap of the halogen substituents by the bulky hydrophilic O-beta-glucosyl substituents; high water solubility is attained only at observed log P octanol approximately 1.5 or lower. Of the new compounds, only 2,4,-6-triiodo-5-N-methylcarboxamidorescorcy bis(beta-glucoside) (6) was highly water soluble. At the physiological pHin dog's plasmia in vitro, compound 6 rapidly hydrolyzed. Poorly water-soluble but more stable compounds of this series were not appreciably absorbed from dog's duodenum.

Animals↗
PubMed1979

Protein--non-ionic detergent interaction. Interaction of bovine serum albumin with alkyl glucosides studied by equilibrium dialysis and infrared spectroscopy.

The binding isotherms of bovine serum albumin with octylglucoside and decyl glucoside were determined at 7 degrees C and 25 degrees C at pH 7.4 and ionic strength 0.1 M. The average number of detergent molecules bound was found to increase with increasing hydrocarbon chain length. Competitive binding indicates that alkylglycosides combine with the same sites as alkyl sulphates. Native bovine serum albumin has about 12 and 10 sites for non-ionic ligands at 7 degrees C and about 15 and 13 sites at 25 degrees C for octyl and decyl glucosides respectively. The values for standard free energy changes--delta G0, were calculated from the intrinsic association constants. Fourier-transformed infrared spectroscopy was used to study the effects of alkyl glucosides on the conformation of albumin. The results obtained indicate that there are no significant changes in protein structure.

Binding, Competitive↗
PubMed1979

Effects of dibutyryl cyclic AMP on the transport of alpha-methyl-D-glucoside and alpha-aminoisobutyric acid in separated tubules and brush border membranes from rabbit kidney.

The effect of dibutyryl cyclic AMP on the transport of alpha-methyl-D-glucoside and alpha-aminoisobutyric acid in separated tubules and purified brush border membranes from rabbit kidney was investigated using a rapid filtration procedure. Dibutyryl cyclic AMP stimulated the uptake of alpha-methyl-D-glucoside and alpha-aminoisobutyric acid by separated renal tubules in agreement iwth prior studies utilizing renal slices (Rea, C. and Segal, S. (1973) Biochim. Biophys. Acta 311, 615--624; Weiss, I.W., Morgan, K. and Phang, J.M. (1972) J. Biol. Chem. 247, 760--764). However, in contrast to previous reports, no preincubation of the tissue with dibutyryl cyclic AMP was required for stimulation of transport to be manifest. Dibutyryl cyclic AMP stimulated oxygen consumption by separated tubules suggesting that stimulation of transport may occur by a linkage with renal oxidative metabolism. Dibutyryl cyclic AMP increased the uptake of alpha-aminoisobutyric acid into purified renal brush border membranes. However the uptakes of alpha-methyl-D-glucoside, proline, leucine and phosphate into brush border membranes were significantly inhibited.

Aminoisobutyric Acids↗
PubMed1978

Identification, properties, and genetic control of UDP-glucose: cyanidin-3-rhamnosyl-(1 leads to 6)-glucoside-5-O-glucosyltransferase isolated from petals of the red campion (Silene dioica).

An enzyme catalyzing the transfer of the glucosyl moiety of UDP-glucose to the 5-hydroxyl group of cyanidin-3-rhamnosyl-(1 leads to 6)-glucoside has been demonstrated in petal extracts of Silene dioica plants. This glucosyltransferase activity was not detectable in green parts of these plants. The enzyme activity is controlled by a single dominant gene M; no glucosyltransferase activity could be demonstrated in petals of m/m plants. The enzyme was purified eightyfold by PVP and Sephadex G50 chromatography. The glucosyltransferase had a pH optimum of 7.4, had a molecular weight of about 55,000, was stimulated by divalent metal ions, and had a "true Km" values of 0.5 x 10(-3) M for UDP-glucose and 3.6 x 10(-3) M for cyanidin-3-rhamnosylglucoside. Pelargonidin-3-rhamnosylglucoside also could serve as acceptor. The enzyme did not catalyze the glucosylation of the 5-hydroxyl group of cyanidin-3-glucoside, although in petals of M/- n/n mutants cyanidin-3,5-diglucoside is present. ADP-glucose could not serve as a glucosyl donor.

Anthocyanins↗
PubMed1977

[Microchemical investigation of alpha D-glucosidases using 4-methylumnelliferyl- and 2-naphthyl-alpha-d-glucoside (author's transl)].

In crude homogenates prepared from freeze-dried cryostate sections of various rat organs the Km and Vmax of acid and neutral alpha-glucosidase as well as the effect of the pH, substrate and enzyme concentration and the incubation time on the activity were determined fluorometrically with 4-methylumbelliferyl- and 2-naphthyl alpha-d-glucoside as substrates. On the basis of the biochemical data 2 assays were developed for the microchemical measurement of both alpha-glucosidases in groups of epithelial cells isolated from freeze dried cryostate sections of the epididymis, jejunum, ilium, liver and kidney of suckling and adult rats. The rate of hydrolysis of 2-naphthyl and 4-methylumbelliferyl alpha-d-glucoside differs moderately. However, due to the higher sensitivity of 4-methylumbelliferone the methylumbelliferyl derivative is preferable especially for the evaluation of alpha-d-glucosidases in cells with low enzyme activity.

Animals↗
PubMed1975

Solubilization of bacterial membrane proteins using alkyl glucosides and dioctanoyl phosphatidylcholine.

The non-ionic detergent octyl glucoside solubilizes a substantial amount of Streptococcus faecalis membrane protein without loss of the monitored enzyme activities. A secondary detergent, dioctanoyl phophatidycholine, appears to increase the yield of solubilized material. In addition, the effect of ionic strength indicates that it may be possible to selectively extract groups of membrane proteins by their characteristic solubility at different ionic strengths. The solubilized membrane-associated enzymes, ATPase and NADH dehydrogenase, enter polyacrylamide gels as distict species. Electrophoretic studies suggest that there are two membrane-associated ATPase in the Streptococcus faecalis, one which dissociates from the membrane in the absence of Mg-2+ ions and the other which remains particulate until solubilized by detergents. Octyl glucoside can be easily removed from a solution containing solubilized proteins and lipid by dialysis.

Adenosine Triphosphatases↗
PubMed1977

Cholesterol beta-D-glucoside-6'-O-palmitate, a metabolite of Pythium sylvaticum.

Cholesterol beta-D-glucoside-6'-O-palmitate has been identified as a polar metabolite in the mycelium of mated cultures of Pythium sylvaticum grown in the presence of cholesterol. The structure was confirmed by synthesis of the metabolite. Similar steroid beta-D-glucoside-6'-O-palmitates were obtained from beta-sitosterol and campesterol when these sterols were added to cultures of P-sylvaticum. Corresponding esters of myristic and stearic acids were also detected.

Cholesterol↗
PubMed1977

Radiopaque contrast media XXXI-Glucoside conjugation of iodophthalein in rabbit.

Report is given on the identification of the metabolites of the iodophthalein sodium (TIP) in rabbit. After i.v. administration two meabolites (S1 and S2) were excreted mostly in the bile, but both were also found in the urine. The TIP glucoronide (S1) is formed in much greater yield than the glucoside (S2). This latter is a further example of glucoside conjugation in mammals.

Animals↗