{"title":"Regulation of cellular polyamines in mammals.","authors":"N Seiler, O Heby","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"23 1","pages":"1-35"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14269182","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":"Low temperature restriction of charge shift in the primary reaction of the bacteriorhodopsin photocycle.","authors":"A K Dioumaev, L Keszthelyi","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Fast electrical signals associated with the primary photoreaction of the bacteriorhodopsin photocycle were studied on dried oriented samples in the temperature range from 77 to 300 K. The rise of the electrical signal, associated with bathointermediate formation, was faster than 5 ns even at 77 K; no slow rising component was detected at any temperature in the nano- to microsecond time range. The amplitude of the signal associated with bathointermediate formation was not affected by cooling from 300 to 210 K, but decreased by a factor of two when the sample was further cooled from 210 to 190 K. At 77 K the amplitude from the first excitation flash is 25-30 per cent of that at 260 K. Our data suggest that low temperature restricts the size of the charge shift during the bathointermediate formation, resulting in creation of a \"low temperature bathointermediate\" distinct from the \"room temperature bathointermediate\".</p>","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"23 3-4","pages":"271-8"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14281220","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":"Summation of unit potentials.","authors":"G Bíró, S Illyés, J Tóth","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The analysis of the compound surface EMG records is directed to obtain information on the activity of motor units. The aim of this study is to contribute to the investigation of the processes taking place in the summation of different unit potentials. The experiments were performed on frog's nerve-muscle preparations. The nerves were stimulated separately and collectively with synchronous and asynchronous electrical impulses. The results obtained by the analysis of the action potentials recorded from the muscles demonstrate that the compound action potentials were brought about by the linear summation of unit potentials involved in the common response.</p>","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"23 3-4","pages":"255-64"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14281218","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 Kecskés, E Palotás, Z Juricskay, L Királyfalvi, M Szécsényi, K Nemes
{"title":"Effect of aeration on cortisol and androgen output by pig adrenal homogenate.","authors":"L Kecskés, E Palotás, Z Juricskay, L Királyfalvi, M Szécsényi, K Nemes","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Of the steroids produced by pig adrenal homogenate, the output of cortisol+11-deoxycortisol, corticosterone, 11 beta-hydroxyandrostenedione, and the steroid intermediates: pregnenolone, 17 alpha-hydroxypregnenolone, progesterone, 17 alpha-hydroxyprogesterone were analysed. The incubations were carried out with and without aeration. Without aeration the oxygen tension in assay medium decreased during incubation in spite of constant shaking. However, it remained constant (140 Hgmm) with aeration throughout the incubation (60 min). The results of steroid analysis demonstrated that the output of 11 beta-hydroxyandrostenedione decreased strongly, and that of cortisol slightly without aeration, however, the output of corticosterone did not change. The addition of 17 alpha-hydroxypregnenolone or 17 alpha-hydroxyprogesterone to the incubation medium eliminated the decrease in the output of cortisol, but not that of 11 beta-hydroxyandrostenedione. The observations suggest that the activation of oxygen in the enzyme reaction catalyzed by 17, 20-lyase, and perhaps by 17 alpha-hydroxylase is weaker than the activation mediated by 21-hydroxylase and 11 beta-hydroxylase.</p>","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"23 1","pages":"37-47"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14269184","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":"Effect of the R46 and PKM101 plasmids on the repair of DNA.","authors":"F Hernádi, I Francia","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"23 1","pages":"83-102"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14269186","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":"Evaluation of ligand induced relative change in the bimolecular quenching constant of protein fluorescence: applications to lysozyme and adenosine deaminase.","authors":"B Somogyi, J Matkó, A Rosenberg","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>By using our model, described in the preceding paper, we investigate the effect of tri-N-acetylglucosamine binding on lysozyme. Furthermore, we reprocess the recently published data (Biochemistry, 1985, 24, 1342) on the effect of different inhibitors on adenosine deaminase. For lysozyme, the inhibitor binding decreases the dynamic accessibility of Trp-108 by changing the dynamics of the protein region separating the buried Trp-108 from the solvent. The reprocessed data on adenosine deaminase-inhibitor systems indicate that the inhibitors which presumably stabilize different (ground or transient) states alter the protein dynamics in both a qualitatively and quantitatively different manner in good agreement with the thermodynamic data of inhibitor binding. Our approach allows us to conclude that ligand induced changes of protein dynamics are not uniform and usually depend on where the protein-ligand complex is situated along the reaction coordinate (or phase-space) and are not localized to the protein groups building up the binding center.</p>","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"23 2","pages":"135-48"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14279292","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":"Vanadate stimulated NADH oxidation in sarcoplasmic reticulum membrane.","authors":"E Molnár, Z Kiss, L Dux, F Guba","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Vanadate stimulated NADH oxidation was detected in sarcoplasmic reticulum membrane preparations. The reaction showed enzymatic character, with half maximal activating concentration of 1.2 mM vanadate and maximal NADH oxidation 50 nmol/mg protein/minute. Acidic pH, micromolar free Ca2+ concentration and decavanadate addition increased the rate of NADH oxidation. The described enzyme activity is similar to the ones observed in erythrocyte liver and cardiac plasma membranes. The vanadate stimulated NADH oxidation in sarcoplasmic reticulum preparations does not seem to originate from other contaminating membrane elements. The presence of this enzyme activity in the sarcoplasmic reticulum should be taken into consideration when planning experiments with vanadate, especially when measuring ATPase activity through NADH oxidation with coupled enzymatic assay.</p>","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"23 1","pages":"63-74"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14106719","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":"Defective myo-inositol-1-phosphate synthase production in an inositolless double mutant Neurospora crassa strain.","authors":"A Kiss, M Schablik, A Zsindely, G Szabó","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A slow growing inl+/- mutant was isolated from an inositol dependent (inl) Neurospora crassa strain. The latter strain produces defective myo-inositol-1-phosphate synthase which has residual activity. Inositol, similarly to that found in wild and inl mutant strains, represses the enzyme production in the inl+/- strain as well. Withdrawing inositol from the medium results in derepression of the enzyme synthesis. Derepression is hindered by cycloheximide. Inl+/- character in the double mutant is brought about by overproduction of the defective myo-inositol-1-phosphate synthase.</p>","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"23 3-4","pages":"215-23"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14111885","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":"Activation/dephosphorylation of rabbit muscle glycogen synthase by the catalytic subunits of protein phosphatase-1 and 2A.","authors":"I Farkas, B Tóth, G Vereb, C Csortos, P Gergely","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Glycogen synthase a was purified from rabbit skeletal muscle by a procedure involving heparin-Sepharose chromatography. Glycogen synthase a was phosphorylated by the catalytic subunit of cAMP-dependent protein kinase to give synthase b1. Dephosphorylation and activation of synthase b1 was investigated using the catalytic subunits of protein phosphatase-1 and 2A. The dephosphorylation and activation of synthase b1 was biphasic with a larger rate constant for the initial phase. Analysis of tryptic phosphopeptides of glycogen synthase during the course of dephosphorylation revealed a faster initial phosphate release from site-2 by both phosphatases comparing to sites-1a and 1b. Ligand effects on synthase phosphatase reactions were also studied. Spermine was found to inhibit protein phosphatase-1 activity and to stimulate type-2A phosphatase using synthase b1 as substrate.</p>","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"23 3-4","pages":"231-46"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13992403","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}
T Spasokukotskaja, J Taljanidisz, M Benczur, M Staub
{"title":"5-fluorodeoxyuridine decreases the effect of arabinofuranosyl-cytosine in undifferentiated human B lymphocytes.","authors":"T Spasokukotskaja, J Taljanidisz, M Benczur, M Staub","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>An activated lymphocyte population was isolated from tonsils of 3-6 years old children by density gradient centrifugation. The isolated light density (LD) cells were bearing early B lymphocyte markers and were 5-6 times more active in DNA synthesis than the high density (HD) lymphocytes. It was found that about 70% of CdR was deaminated and converted into dTMP. The cells were very sensitive to araC, but the incorporation of [14C] CdR was twice more sensitive to araC than that of [5-3H]CdR. This effect can be explained by the interconversion of araC into araT nucleotide via the CdR interconversion pathway. This suggestion was also supported by the effect of 5-F-UdR, which decreased the inhibition of DNA synthesis caused by araC. 5-FUdR the inhibitor of thymidylate synthase, possibly decreases the interconversion of araC into araTTP, and its action via a smaller dTTP pool of the cells. Our data suggest, that the sensitivity of cells to araC may depend on the capacity of the CdR----TdR interconversion pathway, which, however, changes during the normal differentiation process of lymphocytes. Thus, the sensitivity of different malignant cells to araC is determined by the differentiation stage at which they were arrested during cell transformation.</p>","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"23 2","pages":"159-73"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14110326","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}