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Biomedical subjects

W Tanner

Publications and source records attributed to W Tanner.

At least 109 records · Page 6Linked to original sources
PubMed1976

Inhibition of the apparent rate of synthesis on the vacuolar glycoprotein carboxypeptidase Y and its protein antigen by tunicamycin in Saccharomyces cerevisiae.

Carboxypeptidase Y from Saccharomyces cerevisiae contains 14% mannose, the only neutral sugar present. An antiserum can be raised in rabbits which reacts with both the protein and the sugar moieties of the enzyme. This antiserum also precipitates yeast invertase and yeast cell wall mannan. Thus carboxypeptidase Y, which is known to be localized in yeast vacuoles, is very probably a mannoprotein. Tunicamycin inhibits the apparent formation of carboxypeptidase Y to a similar extent as that of the externally localized mannoprotein, invertase. No accumulation of an inactive nonglycosylated or partly glycosylated carboxypeptidase Y occurs as determined by the immunoprecipitation technique. Tunicamycin also inhibits the apparent formation of proteinase A, whereas it does not affect the increase in the activities of a number of other enzymes. It is suggested that in the synthesis of glycoproteins there exists a regulatory link between the synthesis of their polypeptide chains and the reactions involved in their glycosylation.

Anti-Bacterial Agents↗
PubMed1975

Formation of lipid-bound oligosaccharides in yeast.

Incubation of a membrane fraction from Saccharomyces cerevisiae with UDP-N-acetyl [14C]glucosamine catalyzes the transfer of N-acetylglucosamine to an endogenous lipid fraction as well as a methanol-insoluble polymer. The glycolipid was shown to separate into three compounds by thin-layer chromatography. The biosynthesis of two of them could clearly be stimuated by the addition of dolichol monophosphate to the incubation mixture. Evidence is presented that the substances are dolichol pyrophosphate derivatives: dolichol pyrophosphate N-acetylglucosamine and dolichol pyrophosphate di-N-acetylchitobiose. The formation of the chitobiose-containing lipid was increased by reincubation of the glycolipid with non-radioactive UDP-N-acetylglucosamine. The same particulate preparation transferred mannose from GDPmannose to dolichol pyrophosphate di-N-acetylchitobiose, giving rise to a lipid-bound oligosaccharide. Molecular weight determination of the oligosaccharide moiety gave a value of 780, which is consistent with a tetrasaccharide containing two mannose subunits attached to di-N-acetylchitobiose. The methanol-insoluble radioactive product obtained in the presence of UDP-N-acetyl[14C]glucosamine was transformed by pronase treatment to a large extent into dialyzable material. It is suggested that the glycolipids described serve as intermediates in the glycosylation of yeast mannoproteins.

Binding Sites↗
PubMed1974

The hexose-proton cotransport system of chlorella. pH-dependent change in Km values and translocation constants of the uptake system.

The proton concentration in the medium affects the maximal velocity of sugar uptake with a K(m) of 0.3 mM (high affinity uptake). By decreasing the proton concentration a decrease in high affinity sugar uptake is observed, in parallel the activity of a low affinity uptake system (K(m) of 50 mM) rises. Both systems add up to 100%. The existence of the carrier in two conformational states (protonated and unprotonated) has been proposed therefore, the protonated form with high affinity to 6-deoxyglucose, the unprotonated form with low affinity. A plot of extrapolated V(max) values at low substrate concentration versus proton concentration results in a K(m) for protons of 0.14 microM, i.e. half-maximal protonation of the carrier is achieved at pH 6.85. The stoichiometry of protons cotransported per 6-deoxyglucose is close to 1 at pH 6.0-6.5. At higher pH values the stoichiometry continuously decreases; at pH 8.0 only one proton is cotransported per four molecules of sugar. Whereas the translocation of the protonated carrier is strictly dependent on sugar this coupling is less strict for the unprotonated form. Therefore at alkaline pH a considerable net efflux of accumulated sugar can occur. The dependence of sugar accumulation on pH has been measured. The decrease in accumulation with higher pH values can quantitatively be explained by the decrease in the amount of protonated carrier. The properties of the unprotonated carrier resemble strikingly the properties of carrier at the inner side of the membrane. The inside pH of Chlorella was measured with the weak acid 5,5-dimethyl-2, 4-oxazolidinedion (DMO). At an outside pH of 6.5 the internal pH was found to be 7.2. To explain the extent of sugar accumulation it has to be assumed that the membrane potential also contributes to active sugar transport in this alga.

Biological Transport↗
PubMed1974

Regulation of Hexose Transport in Chlorella vulgaris: Characteristics of Induction and Turnover.

Of nine species of unicellular algae tested, Chlorella vulgaris showed the highest inducibility for an active hexose transport system. Whereas the rate of uptake in all other species was increased by induction less than 5-fold, it was increased more than 400-fold in one strain of C. vulgaris. With glucose as inducer, the minimum time necessary to synthesize inducible proteins of the transport system was 15 minutes. The Km for induction with glucose is 5 mum and with 6-deoxyglucose 1 mm. The inducing sugars have to penetrate the cells to be effective.Evidence indicating that regulation of induction occurs at the transcriptional level was obtained. The induction was inhibited by 6-methylpurine. When cells were exposed to induce in the presence of actidione no increase in transport activity could be measured. After removal of actidione as well as the inducer, an increased uptake activity was observed after 30 to 60 minutes. The induced uptake system showed a turnover with a half-life of 4 to 6 hours at 26 C under nongrowing conditions; at 0 C turnover was negligible. Turnover was partly inhibited by anaerobic condition and by actidione; it was accelerated under growing conditions.

Journal Article↗
PubMed1974

Properties of glucosyltransferase and glucan transferase from spinach.

A glucosyl and a glucosyl-glucan transferase activity from spinach (Spinacia oleracea L. var. Matador) leaves have been partially purified and characterized. The latter activity (fraction 1 after diethylaminoethylcellulose chromatography) is responsible for the transfer of glucosyl as well as of maltosyl, maltotriosyl, and higher homologous residues to glucose giving rise to maltose and the correspondingly larger molecules. This fraction also shows beta-amylase activity. The transfer takes place only to glucose; maltose, as well as other alpha-1,4-glucans, serve as donors. The enzyme fraction 2 is amylase-free and catalyzes only the transfer of glucosyl moieties, again with high acceptor specificity to glucose. Maltose and larger alpha-1, 4-glucans, with the exception of maltotriose and maltotetraose, act as donors. The physiological function of these enzymes may be the formation of oligosaccharide primers for starch synthetase or phosphorylase.

Journal Article↗
PubMed1973

The role of cyclic photophosphorylation in vivo.

When cyclic photophosphorylation is inhibited in Chlorella vulgaris cells by carbonylcyanide-trifluoromethoxy phenylhy-drazone, photosynthetic CO(2)-fixation under anaerobic conditions exhibits a distinct lag. Under the same conditions, the light-dependent formation of ribulose diphosphate shows also this lag. It is concluded that cyclic photophosphorylation is required to fill up the pools of phosphorylated intermediates of the Calvin cycle at a time when noncyclic photophosphorylation cannot yet efficiently operate. Under aerobic conditions, the initial energy demand can be accommodated by respiratory ATP or cyclic photophosphorylation or both. Evidence for stoichiometric participation of cyclic photophosphorylation in photosynthesis is still lacking.

Journal Article↗