{"title":"[Effect of cations and DNP on ATPase activity in different tissue fractions of birds' brains].","authors":"A A Simonian, R A Stepanian, G G Batikian","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>ATP-ase activity and the effect of cations (Na+, K+, Mg2+, Ca2+) and DNP on its activity have been studied in avian brain homogenates and mitochondrial and supernatant fractions (microsomes + hyaloplasma). Highest levels of Na+ + K+ -stimulated ATP-ase activity has been shown in avian brain crude mitochondrial fraction, next in supernatant and lowest in homogenates. Following three-fold freezing and thawing, enzyme activity in homogenates and mitochondrial fractions increases considerably and decreases in the supernatant. Highest Mg2+ -stimulated ATP-ase activity is found in avian brain homogenates, next in mitochondrial fractions and supernatants. Mg2+ -stimulated ATP-ase activity is not changed considerably following three-fold freezing and thawing of brain preparations. Highest Ca2+ -stimulated ATP-ase activity has been observed in the supernatant fraction and its activity is considerably reduced following freezing and thawing. Avian brain mitochondrial fractions have high DNP-stimulated ATP-ase activity. Following freezing and thawing of brain preparations DNP-stimulated ATP-ase activity is not changed considerably. The results obtained indicate that in avian brain homogenates and other preparations, cation and DNP-stimulated ATP-ase have different activities. Three-fold freezing and thawing of brain tissue preparations affect these activities differentially.</p>","PeriodicalId":76813,"journal":{"name":"Voprosy biokhimii mozga","volume":"9 ","pages":"219-26"},"PeriodicalIF":0.0,"publicationDate":"1974-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15389938","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"[Changes in the terminal oxidation and active transport of calcium ions in the cerebral mitochondria of white rats following chronic cerebroside administration].","authors":"E E Mkheian, O P Sotskiĭ, E S Sekoian","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Terminal oxidation and active Ca ion transport have been studied in rat brain mitochondria following intraperitonial administrations of cerebrosides for 30 days. The results obtained have shown that cerebrosides inhibit terminal respiration at its 3rd metabolic state and reduce the rate of phosphorylation. ADP/O and ATP/t coefficients decrease due to the active transport of Ca ions. On increasing ADP and CaCl2 the time necessary for the binding and release of hydrogen ions is prolonged.</p>","PeriodicalId":76813,"journal":{"name":"Voprosy biokhimii mozga","volume":"9 ","pages":"227-32"},"PeriodicalIF":0.0,"publicationDate":"1974-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15571992","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
G S Khachatrian, A A Antonian, A A Alaverdian, F A Sarkisian
{"title":"[Ribonuclease and DNA-dependent-RNA-polymerase activity in the brain under normal physiologic conditions].","authors":"G S Khachatrian, A A Antonian, A A Alaverdian, F A Sarkisian","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Ribonuclease activity of nuclear, ribosomal and soluble fractions and DNA linked RNA polymerase activity of rat brain has been studied following alimentary, conditioned alimentary stimulation and conditioned alimentary inhibition. During alimentary and conditioned alimentary stimulation ribonuclease activity is considerably reduced at pH 5.4; 6.0; 7.9 and 8.1 but not at pH 7.6. Under these same conditions ribonuclease activity is high in soluble fraction. DNA-linked RNA-polymerase activity increases during stimulation. During conditioned alimentary inhibition ribonuclease activity of various subcellular fractions is also reduced. Ribonuclease activity of soluble fraction is lower than that observed during stimulation. During inhibition DNA-dependent RNA-polymerase activity is also significantly raised. The significant reduction of ribonuclease activity of nuclear and ribosomal fractions and the significant increase of DNA-dependent RNA-polymerase activity in the nuclear fraction during stimulation and inhibition of brain activity indicate the importance of RNA-polymerase and the biosynthesis of different kinds of RNA during activity of higher brain centers.</p>","PeriodicalId":76813,"journal":{"name":"Voprosy biokhimii mozga","volume":"9 ","pages":"151-70"},"PeriodicalIF":0.0,"publicationDate":"1974-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15571985","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
G K Buniatian, V B Egian, G A Turshian, G E Akopian, S S Safrazian
{"title":"[Glutamine synthetase and glutaminase activity in the brain and liver homogenates and subcellular fractions of rats with alloxan diabetes (3)].","authors":"G K Buniatian, V B Egian, G A Turshian, G E Akopian, S S Safrazian","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Glutaminsynthetase activity has been determined in microsomal and soluble fractions of brain and liver of normal and alloxan diabetic rats and glutaminase activity in homogenates and mitochondrial fractions. The results obtained indicate that in brain of diabetic animals glutaminesynthetase activity of microsomal fractions is changed very slightly while that of the soluble fraction is marked reduced. In liver tissue enzyme activity is significantly decreased in both microsomal and soluble fractions. In homogenates of brain tissue of diabetic animals glutaminase does not differ markedly from that of control animals both in the presence and absence of activators (phosphate, aspartate, bicarbonate). In homogenates of liver, in the absence of activators, glutaminase activity is greater in diabetic animals than in controls, it is not much changed in the presence of phosphate and decreases in the presence of bicarbonate and aspartate. In diabetic animals, in the presence of phosphate, glutaminase activity of brain mitochondrial fractions increases while that of liver mitochondrial fractions does not change. It is interesting to note that in the absence of activators glutaminase activity is absent in both brain and liver mitochondria while it is quite high in homogenates.</p>","PeriodicalId":76813,"journal":{"name":"Voprosy biokhimii mozga","volume":"9 ","pages":"17-24"},"PeriodicalIF":0.0,"publicationDate":"1974-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15267316","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"[Intracellular influence of different mediators on acid ribonuclease activity in brain tissue].","authors":"N N Demin, G A Nechaeva","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The effect of acetylcholine, norepinephrine, serotonin, GABA and histone preparations on nervous tissue acid ribonuclease activity has been studied. Acetylcholine and serotonin in vitro were found to reduce the leakage of this enzyme out of lysosomes, whereas norepinephrine and histones enhanced it. These agents did not change free acid ribonuclease activity. It is assumed that these neurotransmitters and histones can take part in the regulation of intracellular RNA metabolism in brain tissue by changing the amount of the free acid ribonuclease fraction through affecting lysosome membranes rather than the activity of the free enzyme. GABA changes neither enzyme leakage out of lysosomes nor its activity.</p>","PeriodicalId":76813,"journal":{"name":"Voprosy biokhimii mozga","volume":"9 ","pages":"171-5"},"PeriodicalIF":0.0,"publicationDate":"1974-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15267317","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"[Phospholipid composition of the proteolipids of the white matter of different brain and spinal cord regions and of the sciatic nerve in dogs].","authors":"K G Manukian, G K Buniatian","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":76813,"journal":{"name":"Voprosy biokhimii mozga","volume":"9 ","pages":"87-108"},"PeriodicalIF":0.0,"publicationDate":"1974-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15483961","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
K G Manukian, L G Kirakosian, K L Levonian, V N Zakharian
{"title":"[Quantitative changes in the protein of proteolipids in different portions of the nervous system and in the heart during rat ontogenesis].","authors":"K G Manukian, L G Kirakosian, K L Levonian, V N Zakharian","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":76813,"journal":{"name":"Voprosy biokhimii mozga","volume":"9 ","pages":"109-21"},"PeriodicalIF":0.0,"publicationDate":"1974-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15571980","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
V S Oganesian, G K Buniatian, K S Mikirtumova, R L Airapetian
{"title":"[Effect of thiol reagents on cerebral glutaminase activity].","authors":"V S Oganesian, G K Buniatian, K S Mikirtumova, R L Airapetian","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>It has been shown that the glutaminase activity of brain mitochondrial fractions, which is stimulated by various activators, is completely abolished on 10 min preincubation with parachlormercurybenzoate, 5,5'-dithiobis-(2-nitrobenzoate), N-ethylmaleimide, iodoacetamid, CdCl2, ZnCl2 and CuCl2. With the purpose of elucidating the role of SH-groups in glutaminase activity we have studied the possibilities of preventing loss of enzyme activity by substrates and activators. We have shown that glutamine is effective only in the case of CuCl2. It should be noted that preincubation of brain mitochondrial fractions with activators greatly reduces the inhibitory effects of thiol reagents. Besides, activators differ in their effect in preventing glutaminase inactivation by various SH-reagents. After preincubation of glutaminase with activators their protective effect depends on whether glutamin is added together with the inhibitor or after some time. In one case their protective effect increases, in the other decreases and in the third case remains unchanged. On the basis of the data obtained the authors conclude that SH groups of brain glutaminase are not present in the active center and have an important functional significance for its catalytic active conformation.</p>","PeriodicalId":76813,"journal":{"name":"Voprosy biokhimii mozga","volume":"9 ","pages":"5-16"},"PeriodicalIF":0.0,"publicationDate":"1974-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15576180","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
L N Arakelian, A A Demirchian, A M Petrosian, E K Kazarova, N A Esaian
{"title":"[Effect of gamma-aminobutyric acid on the concentration of noradrenaline in the synaptosoma fraction of the meso-diencephalic region of rat brain].","authors":"L N Arakelian, A A Demirchian, A M Petrosian, E K Kazarova, N A Esaian","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>We had previously shown [1, 2, 3, 4] that intraperitoneal administrations of 5 mg/kg amounts of gamma-aminobutyric acid (GABA) lower norepinephrine (NE) level of rat brain, this effect being most pronounced in the hypothalamic region. Subsequent studies showed that GABA increased normetanephrine level in iproniazid pretreated rats (II) and decreased NE content of crude mitochondrial fractions (12). These data implied changes in NE content of nerve endings. The results of the present study indicate that the NE content of the synaptosomal fraction of the mesodiencephalic region of GABA treated rats is significantly lower than that of untreated animals. This is a further confirmation of our previous results favouring a release of NE from nerve endings following the administration of GABA.</p>","PeriodicalId":76813,"journal":{"name":"Voprosy biokhimii mozga","volume":"9 ","pages":"197-202"},"PeriodicalIF":0.0,"publicationDate":"1974-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15267320","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"[Changes in the activities of NAD- and NADP-specific isocitrate dehydrogenases in the brain and liver during the postembryonic development of animals].","authors":"M I Prokhorova, F E Putilina, N D Eshchenko","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The activities of NAD- and NADP-specific isocitrate dehydrogenases (ICDH) were investigated in subcellular fractions of rat brain and liver. Animals of different age groups were used: newborn, 10-, 20-, 30-, 40-days old and adult rats. It was shown that NAD-ICDH activity rose sharply in adult brain mitochondria as compared with that of developing animals. The NAD-dependent pathway of isocitrate oxidation predominated in mitochondria of both developing and adult brain. The activity of NADP-ICDH decreased in brain mitochondria and cytoplasm in the course of development. Some changes in the distribution of enzyme activity between subcellular fractions were also found in adult brain. The activity of mitochondrial NADP-ICDH was higher than that of newborn animals.</p>","PeriodicalId":76813,"journal":{"name":"Voprosy biokhimii mozga","volume":"9 ","pages":"211-8"},"PeriodicalIF":0.0,"publicationDate":"1974-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15267324","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}