{"title":"Effects of skeletal muscle myosin light chain phosphorylation on synthetic actomyosin ATPase activity and superprecipitation.","authors":"I Kalapos, D Stepkowski, S Csabina, A Szöór","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>In the present study the effect of phosphorylation of skeletal muscle myosin light chains on the interaction between myosin and actin has been investigated. The actomyosin ATPase activities were determined for synthetic actomyosins formed from either phosphorylated or non-phosphorylated myosin and pure actin, with the help of the luciferin-luciferase system. The contractile properties of our preparations were simultaneously studied by the superprecipitation model. Phosphorylated form of myosin had lower actin-activated ATPase activity at particular conditions studied. In agreement with this, superprecipitation of phosphorylated actomyosin was delayed. On the basis of these results one can expect that phosphorylation of myosin light chains modulates contractile properties of intact skeletal muscle.</p>","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"24 3","pages":"231-43"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13678516","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 dominant substrate of protein kinase C in the extracts of pig granulocytes is a 38 kDa Ca2+/membrane binding protein.","authors":"L Buday, G Farkas, A Faragó","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>In the crude extracts of pig granulocytes the dominant substrate of endogenous protein kinase C was a 38 kDa protein. This protein was found in the cytosolic extract when the cells were sonicated in the presence of EGTA but it was bound to the membrane fraction when the cells were sonicated in the presence of Ca2+. The phosphorylation of the 38 kDa protein was absolutely Ca2+/phospholipid dependent. The behaviour of this protein kinase C substrate indicated that it was a lipocortin.</p>","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"24 1-2","pages":"101-6"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13676396","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}
Y Hirai, M Yamaguchi, S Yamano, K Takehana, A Winnard
{"title":"Small-square (SS) net exists in trout muscle.","authors":"Y Hirai, M Yamaguchi, S Yamano, K Takehana, A Winnard","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The small-square-net form (with the large-square-net form) was clearly observed in brown trout muscle in cross-square-net-section. Fresh adductor mandibularis and dorsal muscle strips, isometrically clamped to prevent contraction, were prefixed in 3% glutaraldehyde, 0.1 M cacodylate, pH 7.4, and post-fixed in 1% osmium tetroxide in veronal acetate buffer at 2 degrees C. The samples were dehydrated, embedded in epon-araldite, cross-sectioned, and stained with uranyl acetate and lead citrate for electron microscopic observation. The sections provided the first clear evidence of the small-square-net form, coexisting with the basket-weave pattern, in fish muscle. In previous experiments, we could not demonstrate the small-square-net pattern convincingly with guppy tissue (Yamaguchi et al., 1985a) which may be more susceptible to chemical or physical stress than is trout tissue. The existence of the diverse structural patterns in cross-sections of some, if not all, vertebrate striated muscle must be derived from a basic unit which although it may vary in size among species is structurally identical. The findings agreed with our unified model of narrow and wide Z-line structure (Yamaguchi et al., 1980; Yamaguchi et al., 1985a; Yamaguchi et al., 1985b).</p>","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"24 1-2","pages":"159-63"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13658414","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 polyamines on the carbamoyl-phosphate synthase activity of CAD protein.","authors":"Z Szondy, G Matyasi, P Elödi","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The effects of polyamines were studied on carbamoyl-phosphate synthase II (EC 6.3.5.5.) which is the first and rate limiting enzyme in mammalian pyrimidine synthesis. Polyamines in physiological concentrations (0.1-1 mM) strongly inhibited the carbamoyl-phosphate synthesis. Of the polyamines tested spermine was the most effective followed by spermidine and putrescine. Spermine increased the KM for ATP and the requirement for Mg++ of carbamoyl-phosphate synthase reaction. UTP, an inhibitor, had similar, while phosphoribosyl-pyrophosphate, an activator of the enzyme had an opposite effect. Increasing concentrations of phosphoribosyl-pyrophosphate completely reversed the inhibition caused by spermine, while did not influence the degree of inhibition caused by UTP. A possible physiological role of polyamines in synchronizing the substrate and activator functions of phosphoribosyl-pyrophosphate in pyrimidine synthesis is suggested.</p>","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"24 1-2","pages":"107-17"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13628962","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":"Prediction of surface loops of protein-folds from multiple alignments of homologous sequences.","authors":"L Patthy","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Multiple alignments of distantly related homologous sequences may be used for the construction of consensus sequences that identify conserved motifs, variable segments and regions that tolerate gap events. It is suggested that such consensus sequences may be used for the prediction of key features of protein-folds. The validity of the proposed approach is illustrated in the case of the alpha 2 mu globulin superfamily: the consensus sequence derived from the multiple alignment of sequences succeeded in identifying conserved structural motifs and in predicting the location of surface loops that connect these motifs.</p>","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"24 1-2","pages":"3-13"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13628963","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":"Rotational motion of spin labelled microtubule protein.","authors":"M S Kellermayer, K Trombitás, J Belágyi","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Microtubule protein, isolated from porcine brain by temperature-dependent assembly-disassembly cycles, was labelled with two types of nitroxide spin labels, maleimide and isothiocyanate. Labelling was performed either in depolymerized or polymerized form of the protein. Electron paramagnetic resonance spectroscopic measurements revealed 34 ns rotational correlation time of the labels in disassembled microtubule protein which corresponds most likely to the rotational motion of the subunits. Upon polymerization, changes in the rotational dynamics of microtubule protein occurred in the temperature range of 20-30 degrees C. Polymerization process was revealed as a transition between two states, one characterizing the tubulin in its monomeric form and the other the polymeric form. In the temperature range of 20-30 degrees C, both forms (monomer-polymer) of tubulin were observed. Very slow rotational motion in the millisecond time range was detected in microtubule pellet. Orientation dependence in the distribution of spin labels in macroscopically oriented microtubules was not found.</p>","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"24 3","pages":"213-29"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13706211","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 N-ethylmaleimide treatment on naloxone binding in frog brain membranes.","authors":"J Zawilska, A Lajtha, A Borsodi","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Specific binding of (3H) naloxone to opioid receptors in frog (Rana esculenta) brain membranes was irreversibly inactivated by the sulfhydryl group alkylating agent N-ethylmaleimide (NEM). Saturation analysis of (3H) naloxone binding revealed a marked reduction in the number of ligand binding sites after N-ethylmaleimide treatment. Pretreatment of the membranes with unlabelled opioid ligands, i.e. naloxone, morphine, or the kappa selective dynorphin (1-13), and sodium ions resulted in considerable protection of (3H) naloxone binding against the N-ethylmaleimide blockade.</p>","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"24 1-2","pages":"33-9"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13718233","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":"N-ras mutation in chemically induced rat brain tumour.","authors":"P Rády, A R Kinsella, M Fox, I Arany, P Kertai","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Rat brain tumour was induced by treatment with N-ethyl-nitrosourea. Using Southern blot analysis, restriction fragment length polymorphism of N-ras gene was identified. Comparative studies showed that new restriction site did not occur in the DNA of DMN induced renal and liver tumours. The data suggest that the mutation occurring may be specific to the \"target\" cell or to the structure of carcinogens.</p>","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"24 4","pages":"313-6"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13719870","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 role of water in the radiation sensitization of acetone.","authors":"L Gazsó, A Dám","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>These experiments were aimed at the better understanding of the mechanism of the enhancement of radiation damage brought about by acetone in spores of Bacillus megaterium. Particularly, the intention was to examine the extent of involvement of water content in this action of acetone. The radiosensitization of acetone increased with increasing oxygen concentration and ultimately became zero at 2.1% O2 in N2. The extent of sensitization increased with rising concentration of acetone up to the first peak (50% acetone in water) under anaerobic condition. Further increase in acetone concentration resulted a maximum response seen at 90% acetone in water. To investigate the role of hydroxyl radical in the radiation sensitization caused by acetone two different types of hydroxyl radical scavengers (t-butanol and iso-propanol) were used.</p>","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"24 3","pages":"283-90"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13706212","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":"Coupled enzymatic reactions measured in a single protein crystal from myogen A.","authors":"T Keleti, R Berni, M Vas, A Mozzarelli, G L Rossi","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Pairwise coupled reactions of fructose-1,6-bisphosphate aldolase and sn-glycerol-3-phosphate dehydrogenase, 3-phosphoglycerate kinase and D-glyceraldehyde-3-phosphate dehydrogenase, triosephosphate isomerase and sn-glycerol-3-phosphate dehydrogenase have been detected by microspectrophotometry in single crystals obtained from myogen A in the presence of polyethylene glycol. Microspectrophotometric measurements with polarized light demonstrate that the protein molecules are oriented and that NADH is bound with a definite orientation to the dehydrogenases within the crystal.</p>","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"24 1-2","pages":"15-23"},"PeriodicalIF":0.0,"publicationDate":"1989-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13658413","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}