Peter Rysavy

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The phosphorylated proteins of Streptomyces albus, radioactively labeled with [32P]orthophosphate have been analyzed by gel electrophoresis and autoradiography. More than 10 protein species were found to be phosphorylated. With [32P]ATP as substrate cell free extracts phosphorylated endogenous proteins in vitro which were predominantly phosphorylated in(More)
Most nuclearly encoded mitochondrial proteins are synthesized with an amino-terminal leader peptide that is cleaved by the mitochondrial processing peptidase (MPP). Purified rat liver MPP, like the Neurospora and yeast enzymes, consists of two nonidentical subunits, alpha (55 kDa) and beta (50 kDa). To confirm the functional authenticity of the recently(More)
Rat liver mitochondrial processing peptidase (MPP) is the primary peptidase that cleaves leader peptides from nuclearly encoded mitochondrial proteins following their transport from the cytosol to the mitochondrial matrix. This enzyme consists of two nonidentical subunits that have overall similarity to each other and share certain amino acid motifs. These(More)
Protein phosphorylation was investigated inStreptomyces lincolnensis underin vivo conditions. In cells grown in the presence of32P-orthophosphate, proteins ofM=12, 22, 45, 68 and 90 kDa were labeled with32P (detected by gel electrophoresis and autoradiography). These proteins were shown to contain O-phosphoserine and a small proportion of O-phosphotyrosine.(More)
The activity of β-galactosidase during incubation of soil with lactose was studied. Enzyme activity reached its maximum between 6–24 h incubation. The addition of secondary ammonium phosphate stimulated the enzyme formation. Casein hydrolysate alone did not influence significantly enzyme formation even after a 72 h incubation. Enzyme activity in the(More)
The microflora of the chernozem soil mineralized 62% of the lactose retained on a column consisting of three 10-g layers of the soil at a daily flow of 48 mg of the sugar. Only 45% of the sugar was mineralized when the daily flow was 136 mg. The highest value of the beta-galactosidase activity in the system of heterocontinuous cultivation was two-fold with(More)
beta-D-glucosidase in Streptomyces granaticolor is an inducible enzyme. Methyl-beta-D-glucoside or cellobiose, added to a glycerol-containing medium, are most suitable inducers. The activity of beta-D-glucosidase in a culture fully induced by cellobiose is 50 times higher than the basal level of the enzyme. beta-D-glucosidase is an intracellular enzyme,(More)