PubMed Health⌕ Search

Biomedical subjects

L A Novikova

Publications and source records attributed to L A Novikova.

At least 37 records · Page 2Linked to original sources
PubMed1982

[Mitochondrial proteinases of the yeast Saccharomyces cerevisiae: electrophoretic detection, substrate specificity and sensitivity to inhibitors].

The proteins of submitochondrial particles solubilized with 0.1% Triton X-100 were separated by polyacrylamide gel electrophoresis. Hydrolysis of several proteinase substrates was registered directly in the gel after completion of electrophoresis. According to the data obtained the inner mitochondrial membrane contains one or two enzymes which catalyze hydrolysis of cytochrome c as well as one or two enzymes splitting synthetic substrate of trypsin-like proteinases, e. g. N-alpha-benzoyl-L-arginine-p-nitroanilide (BAPA) and N-alpha-benzoyl-L-arginine-beta-naphthylamide (BANA). Submitochondrial particles were shown to catalyze hydrolysis of 3H-labelled cytochrome c. This activity is suppressed by the same inhibitors as the hydrolysis of mitochondrial translation products, i. e. phenyl-methylsulfonylfluoride, p-chloromercuribenzosulfonate, leupeptin and antipain. Presumably these two processes are catalyzed by the same enzyme localized in the inner mitochondrial membrane. Physiological functions of BAPA- and BANA-hydrolyzing enzyme(s) are still unclear.

Kinetics↗
PubMed1982

[Changes in proteinase A and B activity during glucose repression in the yeast Saccharomyces cerevisiae].

The divisible and indivisible yeast S. cerevisiae were subjected to glucose repression by increasing the glucose content in the growth medium up to 10%. Under these conditions the total activities of both proteinases did not change significantly, while those of free (i.e. not bound to natural inhibitors) proteinases were increased manyfold. This effect is probably due to liberation of the proteinases from the vacuoles and digestion of cytosolic proteinase inhibitors.

Aspartic Acid Endopeptidases↗
PubMed1980

[Mitochondrial proteinase of yeast splitting the products of mitochondrial translation].

It has been shown that mitochondria of the yeast Saccharomyces cerevisiae contain proteinase, which is bound to the inner mitochondrial membrane and catalyzes the hydrolysis of mitochondrial translation products in vitro. The efficiency of proteolysis depends on the state of mitochondria: e.g. the degradation of completely formed organelles corresponding to stationary cells, is twice as low as compared to the "young" organelles typical for the beginning of a logarithmic phase of growth. The proteolysis of mitochondrial translation products can occur not only in mitochondria, but also in "inside out" submitochondrial particles. In order to prove the absence of concomitant vacuolar proteinases in preparations of mitochondria and submitochondrial particles, the specific antisera against proteinases A and B have been used. The activity of mitochondrial proteinase is completely inhibited by the natural peptide inhibitors antipain and chymostatin. Of special importance is the fact that another natural peptide inhibitor--leupeptin, having no effect on the activities of vacuolar proteinases, significantly decreases the rate of hydrolysis of mitochondrial translation products. The role of yeast mitochondrial proteinase in regulation of mitochondrial formation is discussed.

Antipain↗
PubMed1979

Proteolysis of the products of mitochondrial protein synthesis in yeast mitochondria and submitochondrial particles.

Degradation of mitochondrial translation products in Saccharomyces cerevisiae mitochondria was studied by selectively labelling these entities in vivo in the presence of cycloheximide and following their fate in isolated mitochondria. One-third to one-half of the mitochondrial translation products are shown to be degraded, depending on the culture growth phase, with an approximate half-life of 35 min. This process is shown to be ATP-dependent, enhanced in the presence of puromycin and inhibited by chloramphenicol. Further, the proteolysis is suppressed by detergents and is insensitive to antisera against yeast proteinases A and B when measured in mitochondria or 'inside-out' submitochondrial particles. It is concluded that the breakdown of mitochondrial translation products is most probably due to the action of endogenous proteinase(s) associated with the mitochondrial inner membrane. This proteinase is inhibited by phenylmethanesulphonyl fluoride, leupeptin, antipain and chymostatin.

Adenosine Triphosphate↗
PubMed1975

[Immunoautoradiographic determination of beta-1 gamma globulin in the blood serum of patients with trophoblastic tumors].

The authors determined beta1-G-globulin (beta1GG) in the sera of patients with different malignant tumours and of normal donors by means of the immunodiffusion method (ID) and immunoautoradiography (IAR). In the ID-negative sera beta1GG was revealed by means of IAR in 7 out of 8 patients with chorionepithelioma of the uterus and in 1 out of 7 patients with teratomblastoma of the testis before the treatment. After the treatment the beta1GG was determined in 7 out of 21 patients with chorionepithelioma of the uterus. At the early stage of trophoblastic tumours of the uterus beta1GG could be found in 77.7% of cases by means of IAR and in 16.8% of cases by means of the ID method.

Autoradiography↗