{"title":"[Effect of neurohormone \"C\" on adenine nucleotide and adenosine metabolism in rat heart and brain].","authors":"A A Galoian, B Ia Guvrits, R G Galstian","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Adenine nucleotides and adenosine are known to be of importance in the regulation of coronary function. This made a study of the effect of neurohormone \"C\" on the metabolism of adenine nucleotides and adenosine interesting in as much as neurohormone \"C\" dilates coronary vessels and has a direct metabolic effect on cardiac muscle. The results obtained have shown that incubation of cardiac muscle homogenates with labelled ATP increased the content of adenosine through raising 5'-AMP nucleotidase activity and inhibiting adenosine deaminase activity. In homogenates and slices of brain tissue the content of adenosine is, on the contrary, reduced. Opposite changes are observed in the content of AMP. The increase of adenosine in the heart by the increase of 5'-AMP nucleotidase activity and decrease of adenosine deaminase activity is probably, not the main factor of the coronarodilatatory effect of neurohormone \"C\". The reverse phenomena is noticed in brain, the functional significance of which must be studied. However, the role of adenosine in the mechanism of action of neurohormone \"C\" will become clear after in vivo experiments which are in progress.</p>","PeriodicalId":76813,"journal":{"name":"Voprosy biokhimii mozga","volume":"11 ","pages":"197-207"},"PeriodicalIF":0.0,"publicationDate":"1976-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12212468","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":"[Shifts in several aspects of phospholipid metabolism in the brains of white rats with radiation sickness].","authors":"A A Agababova, K G Karagezian","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Sublethal (400) and lethal (1600) doses of roentgen decrease the level of neutral phospholipids of rat brain and increase that of acid phospholipids. With the development of radiation disease the content of free glycerine and glycerophosphate increases and the glycerokinase and glycolytic pathways of glycerophosphate biosynthesis are activated together with the intensification of the direct and reverse reactions catalyzed by glycerophosphate dehydrogenase. The permeability of the artificial bimolecular phospholipid membranes prepared from rat brain phospholipid extracts is significantly increased at the end of the radiation.</p>","PeriodicalId":76813,"journal":{"name":"Voprosy biokhimii mozga","volume":"11 ","pages":"129-42"},"PeriodicalIF":0.0,"publicationDate":"1976-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12212689","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 B Egian, G A Turshian, G E Akopian, S S Safrazian, G Kh Buniatian
{"title":"[Rat brain and liver glutamine synthetase and gamma-glutamyltransferase activity in alloxan diabetes (IV)].","authors":"V B Egian, G A Turshian, G E Akopian, S S Safrazian, G Kh Buniatian","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Glutamine synthetase and gamma-glutamyltransferase activities of brain and liver homogenates of rats suffering from alloxan diabetes were determined in the soluble fraction (fraction 1) and in that obtained after treatment with 0.2 percent deoxycholate (fraction 2). The results obtained indicate that the activities of these enzymes in homogenates of brain and liver of diabetic animals does not differ from that of normal animals. gamma-Glutamyltransferase activity of brain is significantly reduced (about 5 fold) in the soluble fraction while glutamine synthetase activity is not much changed. The activities of glutamine-synthetase and gamma-glutamyltransferase of the 2-nd fraction obtained from rat brain and liver are very much higher than in the first fraction and are not considerably different from the activities observed in normal animals. In contrast to brain, glutamine synthetase and gamma-glutamyltransferase activities of liver of diabetic animals do not differ from the activities observed in normal animals, both in the homogenates and in the 1-st and 2-nd fractions.</p>","PeriodicalId":76813,"journal":{"name":"Voprosy biokhimii mozga","volume":"11 ","pages":"29-34"},"PeriodicalIF":0.0,"publicationDate":"1976-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11246592","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}
S G Sharoian, A A Shaldzhian, R M Nalbandian, G Kh Buniatian
{"title":"[Soluble cerebral metalloproteins. 1. Purification and properties of cerebral cortex cytochrome c].","authors":"S G Sharoian, A A Shaldzhian, R M Nalbandian, G Kh Buniatian","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Cytochrome c from grey matter of brain has been obtained as a homogeneous preparation by electrophoresis on polyacrylamide gel and following electrofocusing in ampholine solutions. Its molecular weight, content of iron, redox potential and isoelectric point have been established. The absolute spectra of its oxidized and reduced forms are presented. Cytochrome c of brain cortex is similar in its properties to that obtained from other animal tissues as the heart and adrenal cortex.</p>","PeriodicalId":76813,"journal":{"name":"Voprosy biokhimii mozga","volume":"10 ","pages":"66-74"},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11404145","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":"The electrogenesis and metabolic regulation of slow oscillations underlying burst firing patterns in aplysia and hellix neurons.","authors":"H Wachtel, N T Carnevale, S N Ayrapetyan","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":76813,"journal":{"name":"Voprosy biokhimii mozga","volume":"10 ","pages":"144-67"},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12411376","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":"[AMP-aminohydrolase activity of the nuclear fraction of rat brain].","authors":"L A Manukian, A V Arutiunian","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>AMP-aminohydrolase activity has been found not only in mitochondrial and soluble fractions but also in nuclear fraction of rat brain. The regulation of nuclear AMP-aminohydrolase activity differs from that of mitochondrial and soluble fractions. 1. Hexokinase does not enhance deamination of AMP in intact nuclei while it activates the enzyme in extracts of acetone powder of nuclear fractions. 2. The AMP-aminohydrolase activity of rat brain nuclear fraction is considerably inhibited by GTP and phosphate but in contrast to other fractions the stimulatory effect of ATP on enzyme activity is preserved.</p>","PeriodicalId":76813,"journal":{"name":"Voprosy biokhimii mozga","volume":"10 ","pages":"33-9"},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12411380","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":"Corpus striatum as the site of drug action.","authors":"I J Wajda, A Lajtha","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":76813,"journal":{"name":"Voprosy biokhimii mozga","volume":"10 ","pages":"107-16"},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12411373","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":"[New findings concerning cardiac proteins binding the coronary dilating substances of the hypothalamus].","authors":"R M Srapionian, S S Misirian, A A Galoian","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>We had previously shown that the protein component obtained from heart muscle by 0.1--0.2 saturation with ammonium sulfate exhibits a coronarodilatatory effect. Later on we succeeded in isolating from this protein complex, through dialysis, two coronaoractive low molecular compounds, one of which is apparently a neurohormone. In the present study we isolated, purified and studied the features of this protein complex. The results of gel filtration on Sephadex G-100 confirmed the presence of two different coronaroactive neurohormone binding proteins in heart muscle. The active fractions have been also purified through ion exchange chromatography on diethylaminoethyl cellulose. The purity of these fractions was tested through electrophoresis on 7.5% polyacrylamide gel. In the last stage of purification the active proteins moved towards the anode by one zone.</p>","PeriodicalId":76813,"journal":{"name":"Voprosy biokhimii mozga","volume":"10 ","pages":"122-8"},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12411375","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}
M I Prokhorova, M A Bespalova, A P Mukhina, S Iu Tumanova
{"title":"[Metabolic activity of the N-acetylneuraminic acid of the principle gangliosides of the brain].","authors":"M I Prokhorova, M A Bespalova, A P Mukhina, S Iu Tumanova","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The turnover rate of N-acetylneuraminic acid of brain gangliosides (GT1, GD1b, GD1a, GM1) was studied following the injection of 2-14C-acetate. The specific activity of N-acetylneuraminic acid in GD1a and GM1 was found to be higher than in GD1b. The administration of aminasine reduced the specific activity of N-acetylneuraminic acid whereas chlorhydrate increased that of major brain ganglosides.</p>","PeriodicalId":76813,"journal":{"name":"Voprosy biokhimii mozga","volume":"10 ","pages":"182-6"},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12411377","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":"[Coenzyme specificity and isoenzyme spectrum of lactate dehydrogenase from different regions of the brain].","authors":"S G Movsesian, N O Movsesian","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The coenzyme affinity of lactate dehydrogenase of various parts of rat brain is different to deamino-NAD and NAD as well as to their reduced forms. In direct reactions NAD exhibits a higher activity than deamino-NAD. In the reverse reaction an opposite pattern is observed. The effect of deamino-NADH is much higher than that of NADH. Our studies have shown that the isoenzymes of LDH which are richer in H subunits have a higher affinity for deamino-NAD and deamino-NADH than for NAD and NADH. The isoenzymes of LDH that contain more M forms have opposite properties. LDH-3 does not show a pronounced selective affinity. The data obtained indicate that the activity of LDH and of its 5 isoenzymes varies greatly in different brain parts; crucial changes being observed in the relative percentage of molecular forms of LDH.</p>","PeriodicalId":76813,"journal":{"name":"Voprosy biokhimii mozga","volume":"10 ","pages":"75-83"},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11404148","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}