Helmut Holzer
YOU?
Author Swipe
View article: Laser Treatment of Wood Surfaces for Ski Cores: An Experimental Parameter Study
Laser Treatment of Wood Surfaces for Ski Cores: An Experimental Parameter Study Open
Recently, the production of skis with wooden cores has increased due to changes in customer awareness concerning ecological issues and rising raw material costs for mineral oil resources. The preparation of ski surfaces is one of the main …
View article: Studies on the Regulation and Localization of the Glyoxylate Cycle Enzymes in Saccharomyces cerevisiae
Studies on the Regulation and Localization of the Glyoxylate Cycle Enzymes in Saccharomyces cerevisiae Open
The regulation of the enzymes involved in the operation of the glyoxylate cycle was studied in the yeast Saccharomyces cerevisiae. All enzymes showed an increase in specific activity under growth conditions where the glyoxylate cycle is ne…
View article: Neutral trehalase Nth1p of <i>Saccharomyces cerevisiae</i> encoded by the <i>NTH1</i> gene is a multiple stress responsive protein
Neutral trehalase Nth1p of <i>Saccharomyces cerevisiae</i> encoded by the <i>NTH1</i> gene is a multiple stress responsive protein Open
We have shown previously that expression of the NTH1 gene is increased at heat stress (40°C) both at the mRNA and enzymatic activity levels. This increased expression was correlated to the requirement of the NTH1 gene for recovery after he…
View article: The heat shock factor and mitochondrial Hsp70 are necessary for survival of heat shock in <i>Saccharomyces cerevisiae</i>
The heat shock factor and mitochondrial Hsp70 are necessary for survival of heat shock in <i>Saccharomyces cerevisiae</i> Open
A heat shock recovery assay on solid medium (Nwaka et al. (1995) J. Biol. Chem. 270, 10193–10198) as well as the classical cell counting method were used to investigate the function of some heat shock proteins in thermotolerance. We show t…
View article: Deletion of the <i>ATH1</i> gene in <i>Saccharomyces cerevisiae</i> prevents growth on trehalose
Deletion of the <i>ATH1</i> gene in <i>Saccharomyces cerevisiae</i> prevents growth on trehalose Open
The biological function of the yeast trehalases (EC 3.2.1.28) consists of down‐regulation of the concentration of trehalose via glucose formation by trehalose hydrolysis. While it is generally accepted that the cytosolic neutral trehalase …
View article: Expression and Function of the Trehalase Genes NTH1 and YBR0106 in Saccharomyces cerevisiae
Expression and Function of the Trehalase Genes NTH1 and YBR0106 in Saccharomyces cerevisiae Open
The biological function of the trehalose-degrading yeast enzyme neutral trehalase consists of the control of the concentration of trehalose, which is assumed to play a role in thermotolerance, in germination of spores, and in other life fu…
View article: Phenotypic features of trehalase mutants in <i>Saccharomyces cerevisiae</i>
Phenotypic features of trehalase mutants in <i>Saccharomyces cerevisiae</i> Open
In the yeast Saccharomyces cerevisiae , some studies have shown that trehalose and its hydrolysis may play an important physiological role during the life cycle of the cell. Recently, other studies demonstrated a close correlation between …
View article: Is thermotolerance of yeast dependent on trehalose accumulation?
Is thermotolerance of yeast dependent on trehalose accumulation? Open
During heat stress, trehalose concentration increases in yeast cells in parallel to thermotolerance. This parallelism suggested that trehalose mediated thermotolerance. We show in this work that, under certain conditions, trehalose accumul…
View article: Identification and characterization of a novel yeast gene: the YGP1 gene product is a highly glycosylated secreted protein that is synthesized in response to nutrient limitation.
Identification and characterization of a novel yeast gene: the YGP1 gene product is a highly glycosylated secreted protein that is synthesized in response to nutrient limitation. Open
Nutrient starvation in the yeast Saccharomyces cerevisiae leads to a number of physiological changes that accompany entry into stationary phase. The expression of genes whose products play a role in stress adaptation is regulated in a mann…
View article: Molecular analysis of the neutral trehalase gene from Saccharomyces cerevisiae.
Molecular analysis of the neutral trehalase gene from Saccharomyces cerevisiae. Open
Neutral trehalase (EC 3.2.1.28) is a trehalose hydrolyzing enzyme of the yeast Saccharomyces cerevisiae (App, H., and Holzer, H. (1989) J. Biol. Chem. 264, 17583-17588). The gene of neutral trehalase was cloned by complementation of a neut…
View article: Metabolic regulation of the trehalose content of vegetative yeast
Metabolic regulation of the trehalose content of vegetative yeast Open
We have investigated the mechanism by which heat shock conditions lead to a reversible accumulation of trehalose in growing yeast. When cells of S. cerevisiae MI growing exponentially at 30°C were shifted to 45°C for 20 min, or to 39°C for…
View article: Yeast fructose‐2,6‐bisphosphate 6‐phosphatase is encoded by <i>PHO8</i>, the gene for nonspecific repressible alkaline phosphatase
Yeast fructose‐2,6‐bisphosphate 6‐phosphatase is encoded by <i>PHO8</i>, the gene for nonspecific repressible alkaline phosphatase Open
Yeast fructose‐2,6‐bisphosphate 6‐phosphatase has been purified 7000‐fold by heat treatment, poly(ethylene glycol) precipitation, ion‐exchange chromatography with Q‐Sepharose Fast Flow and Mono Q followed by affinity chromatography with co…
View article: Purification and Characterization of Neutral Trehalase from the Yeast ABYS1 Mutant
Purification and Characterization of Neutral Trehalase from the Yeast ABYS1 Mutant Open
Neutral trehalase was purified from stationary yeast ABYSl mutant cells deficient in the vacuolar proteinases A and B and the carboxypeptidases Y and s.The purified electrophoretically homogeneous preparation of phosphorylated neutral treh…
View article: Characterization of yeast fructose‐2,6‐bisphosphate 6‐phosphatase
Characterization of yeast fructose‐2,6‐bisphosphate 6‐phosphatase Open
To obtain information on the biological significance of yeast fructose‐2,6‐bisphosphate 6‐phosphatase, kinetic data of the purified enzyme [(1987) Eur. J. Biochem. 164, 27–30] have been measured. Maximal activity was found between Ph 6 and…
View article: Purification and characterization of acid trehalase from the yeast suc2 mutant.
Purification and characterization of acid trehalase from the yeast suc2 mutant. Open
Acid trehalase was purified from the yeast suc2 deletion mutant. After hydrophobic interaction chromatography, the enzyme could be purified to a single band or peak by a further step of either polyacrylamide gel electrophoresis, gel filtra…
View article: Mechanism of stimulation of endogenous fermentation in yeast by carbonyl cyanide m-chlorophenylhydrazone.
Mechanism of stimulation of endogenous fermentation in yeast by carbonyl cyanide m-chlorophenylhydrazone. Open
Addition of the uncoupler and protonophore carbonyl cyanide m-chlorophenylhydrazone (CCCP) to starved yeast cells starts endogenous alcoholic fermentation lasting about 20 min. Hexose 6-phosphates, fructose 2,6-bisphosphate, and pyruvate a…
View article: Fructofuranose 2-phosphate is the product of dephosphorylation of fructose 2,6-bisphosphate
Fructofuranose 2-phosphate is the product of dephosphorylation of fructose 2,6-bisphosphate Open
Using comparative ion-exchange chromatography on Dowex 1X4, the product of dephosphorylation of fructose 2,6-bisphosphate with purified yeast fructose-2,6-bisphosphate 6-phosphohydrolase, was shown to be identical to the furanose form of f…
View article: Phosphorylated fructose-1,6-bisphosphatase dephosphorylating protein phosphatase from Saccharomyces cerevisiae.
Phosphorylated fructose-1,6-bisphosphatase dephosphorylating protein phosphatase from Saccharomyces cerevisiae. Open
Phosphorylation of fructose-1,6-bisphosphatase with cyclic AMP-dependent protein kinase from yeast is accompanied by a 50% decrease in the catalytic activity (Pohlig, G. and Holzer, H. (1985) J. Biol. Chem. 260, 13818-13823). Using reactiv…
View article: Mechanism of control of adenylate cyclase activity in yeast by fermentable sugars and carbonyl cyanide m-chlorophenylhydrazone.
Mechanism of control of adenylate cyclase activity in yeast by fermentable sugars and carbonyl cyanide m-chlorophenylhydrazone. Open
The phosphorylation of fructose-1,6-bisphosphatase is preceded by a transient increase in the intracellular level of cyclic AMP which activates a cyclic AMP-dependent protein kinase (Pohlig, G., and Holzer, H. (1985) J. Biol. Chem. 260, 13…
View article: Synergistic effect of<i>m</i>-chloro-peroxybenzoic acid, sulfite and nitrite on the energy metabolism of<i>Saccharomyces cerevisiae</i>
Synergistic effect of<i>m</i>-chloro-peroxybenzoic acid, sulfite and nitrite on the energy metabolism of<i>Saccharomyces cerevisiae</i> Open
The respiration of starved Saccharomyces cerevisiae is inhibited 50% by 0.008 mM, 0.013 mM, or 0.06 mM m-chloro-peroxybenzoic acid (CPBA) when ethanol, glucose, or no external substrate is added, respectively. CPBA concentrations of 0.01–0…
View article: Phosphorylation and inactivation of yeast fructose-1,6-bisphosphatase by cyclic AMP-dependent protein kinase from yeast.
Phosphorylation and inactivation of yeast fructose-1,6-bisphosphatase by cyclic AMP-dependent protein kinase from yeast. Open
Purified fructose-1,6-bisphosphatase from Saccharomyces cerevisiae was phosphorylated in vitro by purified yeast cAMP-dependent protein kinase. Maximal phosphorylation was accompanied by an inactivation of the enzyme by about 60%. In vitro…
View article: Characterization of fructose 1,6-bisphosphatase from bakers' yeast.
Characterization of fructose 1,6-bisphosphatase from bakers' yeast. Open
Active nonphosphorylated fructose bisphosphatase (EC 3.1.3.11) was purified from bakers' yeast. After chromatography on phosphocellulose, the enzyme appeared as a homogeneous protein as deduced from polyacrylamide gel electrophoresis, gel …
View article: Immunochemical studies on catabolite inactivation of phosphoenolpyruvate carboxykinase in Saccharomyces cerevisiae.
Immunochemical studies on catabolite inactivation of phosphoenolpyruvate carboxykinase in Saccharomyces cerevisiae. Open
Phosphoenolpyruvate carboxykinase (EC 4.1.1.49) from Saccharomyces cerevisiae was purified to homogeneity. The enzyme is composed of four subunits of Mr = 64,000. Specific antibodies against phosphoenolpyruvate carboxykinase were raised in…
View article: Purification and properties of proteinase A from yeast.
Purification and properties of proteinase A from yeast. Open
Proteinase A (EC 3.4.23.6) was purified from commercial bakers' yeast in five steps, including hydrophobic chromatography and affinity chromatography. After the last step the enzyme appeared homogeneous on polyacrylamide gel electrophoresi…
View article: Primary structure of yeast proteinase B inhibitor 2.
Primary structure of yeast proteinase B inhibitor 2. Open
The complete amino acid sequence of yeast proteinase B inhibitor 2 (IB2) was determined to be H3N+-Thr-Lys-Asn-Phe-Ile-Val-Thr-Leu-Lys-Lys-Asn-Thr-Pro-Asp-Val-Glu-Ala-Lys-Lys-Phe-Leu-Asp-Ser-Val-His-His-Ala-Gly-Gly-Ser-Ile-Leu-His-Glu-Phe-…