International Journal of Biochemistry最新文献

{"title":"Solubilization, partial purification and functional reconstitution of a sheep brain endoplasmic reticulum anion channel","authors":"A.M. Silvestro,&nbsp;R.H. Ashley","doi":"10.1016/0020-711X(94)90135-X","DOIUrl":"10.1016/0020-711X(94)90135-X","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. An intracellular anion channel, known to be co-localized in brain endoplsmic reticulum membranes with ryanodine-sensitive calcium-release channels, was incorporated into voltage-clamped planar lipid bilayers from sheep brain microsomal membrane vesicles.</p></span></li><li><span>2.</span><span><p>2. Single channels, which displayed a main open-state conductance of 80–100 pS in symmetric 450 mM choline Cl, reduced to ~20pS in symmetric 225 mM (choline)₂ SO₄ (the solutions also contained 10 mM Tris-HCl, pH 7.4), discriminated poorly between Cl⁻ and choline⁺ (relative permeability ratio. P_Cl− /P_chlorine+, 2.5).</p></span></li><li><span>3.</span><span><p>3. Sheep brain microsomal membrane proteins were solubilized in the zwitterionic detergent CHAPS, and subjected to sequential anion-exchange and size-exclusion chromatography; the solubilizate, and partially-purified protein fractions, were then incorporated into large unilamellar liposomes by freeze-thaw sonication.</p></span></li><li><span>4.</span><span><p>4. Reconstituted passive anion (Cl₋)-transport, which was reduced by ~60% in the presence of SO₄²⁻, was assayed by measuring the efflux of entrapped ³⁶Cl⁻ (compared to the efflux of [³H]inulin), and also by monitoring the fluorescence quenching of entrapped SPQ by Cl⁻-influx.</p></span></li><li><span>5.</span><span><p>5. Cl⁻ -transporting activity was enriched up to 200-fold after two stages of purification, and the partially-purified channel protein was incorporated from reconstituted proteoliposomes into planar lipid bilayers, where its permeation behaviour remained very similar to that observed for the native channel.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 9","pages":"Pages 1129-1138"},"PeriodicalIF":0.0,"publicationDate":"1994-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90135-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18985924","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":"Different oxidative pathways of isonicotinic acid hydrazide and its meta-isomer, nicotinic acid hydrazide","authors":"Ben J. van der Walt,&nbsp;Johann M. van Zyl,&nbsp;André Kriegler","doi":"10.1016/0020-711X(94)90130-9","DOIUrl":"10.1016/0020-711X(94)90130-9","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Superoxide was generated during the auto-oxidation of the antituberculous drug, isonicotinic acid hydrazide (INH), but not with its meta-isomer, nicotinic acid hydrazide (NH). During Fe²⁺-stimulated oxidation of INH and NH, aromatic hydroxylation occurred which was inhibited by the chelating agent, phytic acid.</p></span></li><li><span>2.</span><span><p>2. A mixture of myeloperoxidase (MPO) and a hydrazide induced formation of compound III (oxyperoxidase) and aromatic hydroxylation which was stimulated by phytic acid. INH was considerably more potent than NH.</p></span></li><li><span>3.</span><span><p>3. Co-oxidation of a hydrazide and thyroxine (T₄) in the MPO system resulted in the formation of a pink-coloured product (maximum absorbance at 504 nm) which was more stable with NH than with INH.</p></span></li><li><span>4.</span><span><p>4. The hydrazides and Cl⁻ acted synergistically on MPO haem modification when co-oxidised in the MPO-H₂O₂ system. INH was more destructive than NH.</p></span></li><li><span>5.</span><span><p>5. The different oxidative pathways of the hydrazides are consistent with the fact that an acyl intermediate of INH, unlike that of NH, is resonance stabilized.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 9","pages":"Pages 1081-1093"},"PeriodicalIF":0.0,"publicationDate":"1994-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90130-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18983996","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":"Tissue lipoperoxidation and glutathione peroxidase activity in puromycin aminonucleoside injected rats","authors":"José Pedraza-Chaverrí,&nbsp;Ana Elena Arévalo","doi":"10.1016/0020-711X(94)90136-8","DOIUrl":"10.1016/0020-711X(94)90136-8","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Lipoperoxidation (LPx) and glutathione peroxidase (GPx) activity were measured in kidney, liver, heart, lung, brain and testis from control and puromycin aminonucleoside (PAN) injected rats on days 1–6, 8, 10, 16 and 22 after vehicle or PAN injection.</p></span></li><li><span>2.</span><span><p>2. PAN-injected rats developed proteinuria on day 3.</p></span></li><li><span>3.</span><span><p>3. In PAN-injected rats: (a) LPx increased in kidney, liver, lung, brain and testis before day 3 and in heart on day 3; (b) GPx activity increased in kidney, liver, heart, lung and testis and diminished in brain on day 3 or after.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 9","pages":"Pages 1139-1145"},"PeriodicalIF":0.0,"publicationDate":"1994-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90136-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18985925","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 of 3-methyl-branched fatty acids in rat liver","authors":"J.C.T. Vanhooren ,&nbsp;S. Asselberghs ,&nbsp;H.J. Eyssen ,&nbsp;G.P. Mannaerts ,&nbsp;P.P. Van Veldhoven","doi":"10.1016/0020-711X(94)90131-7","DOIUrl":"10.1016/0020-711X(94)90131-7","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Subcellular fractionation of rat liver revealed that 3-methylmargaric acid, a monobranched phytanic acid analogue, can be activated by mitochondria, endoplasmic reticulum and peroxisomes.</p></span></li><li><span>2.</span><span><p>2. Indirect data (effects of pyrophosphate and Triton X-100) suggested that the peroxisomal activation of 3-methylmargaric, 2-methylpalmitic and palmitic acid is catalyzed by different enzymes.</p></span></li><li><span>3.</span><span><p>3. Despite many attempts, column chromatography of solubilized peroxisomal membrane proteins so far did not provide more conclusive data. On various matrices, lignoceroyl-CoA synthetase clearly eluted differently from the synthetases acting on 3-methylmargaric, 2-methylpalmitic and palmitic acid. The latter three however, tended to coelute together, although often not in an identical manner.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 9","pages":"Pages 1095-1101"},"PeriodicalIF":0.0,"publicationDate":"1994-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90131-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18983997","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":"DNase-I-like enzyme from the carp liver—Inhibition by muscle and endogenous actin","authors":"Maria Malicka-Blaszkiewicz,&nbsp;Ilona Majcher,&nbsp;Dorota Nowak","doi":"10.1016/0020-711X(94)90137-6","DOIUrl":"10.1016/0020-711X(94)90137-6","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. DNase-I-like activity occurs in the carp (<em>Cyprinus carpio</em>) liver cytosol (supernatant 105,000<em>g</em>).</p></span></li><li><span>2.</span><span><p>2. The enzyme resembles DNase I from bovine pancreas in respect to the molecular mass (~31 kDa), pH (7.4) and ion requirements (Mg²⁺, Ca²⁺) and the ability to degrade native as well as denatured DNA.</p></span></li><li><span>3.</span><span><p>3. As judged by comparison of DNase zymograms obtained after native- and SDS-PAGE, the enzyme occurs in the three molecular forms of similar molecular weight and different charges.</p></span></li><li><span>4.</span><span><p>4. All these forms are inhibited by rabbit skeletal muscle actin as well as by endogenous actin isolated from the carp liver cytosol.</p></span></li><li><span>5.</span><span><p>5. DNase from the carp liver cytosol does not interact with the antibodies directed against DNase I from bovine pancreas and against DNase I from the rat and bovine parotid glands.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 9","pages":"Pages 1147-1155"},"PeriodicalIF":0.0,"publicationDate":"1994-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90137-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18985926","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":"Transcriptional regulation of environmentally inducible genes in plants by an evolutionary conserved family of G-box binding factors","authors":"Nick C. de Vetten ,&nbsp;Robert J. Ferl","doi":"10.1016/0020-711X(94)90128-7","DOIUrl":"10.1016/0020-711X(94)90128-7","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. In reviewing a number of the most intensely studied environmentally inducible promoters it becomes clear that the presence of two <em>cis</em>-acting elements are critical for promoter activity, one of which is the G-box (CCACGTGG). A mutation in one of the two elements abolishes or severely reduces the ability of the promoter to respond to environmental changes. The sequence of the second <em>cis</em>-acting element, positioned nearby the G-box, is not conserved among the different inducible promoters, but may be similar among promoters induced by the same signal. The spacing between the G-box and the second <em>cis</em>-acting element appears to be critical, suggesting a direct interaction between the respective binding factors. We speculate on a potential role of the G-box promoter element in the signal induction of promoter activity.</p></span></li><li><span>2.</span><span><p>2. From a number of plant species nuclear proteins interacting with the G-box have been identified. Recently, G-box Binding Factors (GBF) have been isolated by screening cDNA expression libraries with a characterized G-box <em>cis</em>-acting element as DNA probe. The deduced amino acid sequence of the GBF clones revealed that they possess the features of the basic leucine zipper class of <em>trans</em>-acting factors. By amino acid sequence comparison and limited mutational analysis, we define amino acids critical for G-box binding specificity. All GBFs isolated to date have a conserved proline-rich domain involved in transcriptional activation. A number of GBFs are inducible by a particular environmental signal.</p></span></li><li><span>3.</span><span><p>3. Recently, a protein designated GF14 has been isolated that is associated with the GBF protein complex. The protein has homology to mammalian brain specific proteins, which seem to function as regulators of phosphorylation events. GBF activity is regulated by phosphorylation. The GF14 proteins may therefore impose an additional control on gene expression.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 9","pages":"Pages 1055-1068"},"PeriodicalIF":0.0,"publicationDate":"1994-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90128-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18983994","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":"Platelet-activating factor acetylhydrolase (PAF-AH) in human kidney","authors":"Smaragdi Antonopoulou ,&nbsp;Constantinos A. Demopoulos ,&nbsp;Christos Iatrou ,&nbsp;George Moustakas ,&nbsp;Panos Zirogiannis","doi":"10.1016/0020-711X(94)90138-4","DOIUrl":"10.1016/0020-711X(94)90138-4","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. PAF-AH activity in human kidney (cortex and medulla) has been demonstrated and shares the following properties.</p></span></li><li><span>2.</span><span><p>2. Does not require the presence of Ca²⁺ and appears to be different from phospholipase A₂.</p></span></li><li><span>3.</span><span><p>3. The pH optimum shows a peak at 7–7.4.</p></span></li><li><span>4.</span><span><p>4. It is stable for 4 days at −30°C.</p></span></li><li><span>5.</span><span><p>5. It is mainly distributed in the microsomal fraction.</p></span></li><li><span>6.</span><span><p>6. The apparent <em>K</em>_<em>m</em>, values of the enzymes of cortex and medulla are 0.553 and 0.207 μM, respectively and distinct from serum PAF-AH (1.439 μM).</p></span></li><li><span>7.</span><span><p>7. The apparent molecular weight values are 60,000 and 25,000 for medulla and cortex, respectively and distinct from serum PAF-AH (94,000).</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 9","pages":"Pages 1157-1162"},"PeriodicalIF":0.0,"publicationDate":"1994-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90138-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18985927","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":"Post-translational and transcriptional regulation of polyamine biosynthesis in Escherichia coli","authors":"Christos A. Panagiotidis,&nbsp;Shu-Ching Huang ,&nbsp;Evangelos S. Canellakis","doi":"10.1016/0020-711X(94)90070-1","DOIUrl":"10.1016/0020-711X(94)90070-1","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Ornithine and arginine decarboxylases (ODC and ADC) of <em>Escherichia coli</em> are inhibited post-translationally by antizyme and ribosomal proteins S20 and L34.</p></span></li><li><span>2.</span><span><p>2. The inhibition of either enzyme is relieved when excess of the other decarboxylase is added.</p></span></li><li><span>3.</span><span><p>3. Using this approach, <em>in vitro</em> as well as <em>in vivo</em>, we demonstrate that the extent of the post-translational inhibition of ODC and ADC in <em>E. coli</em> is at least 65 and 50%, respectively.</p></span></li><li><span>4.</span><span><p>4. The inhibited enzyme levels increase even further upon exposure of cells to polyamines.</p></span></li><li><span>5.</span><span><p>5. The post-translational mode of regulation can counteract a 4-fold increase of ODC protein in the cell.</p></span></li><li><span>6.</span><span><p>6. The negative transcriptional regulation of ODC and ADC expression by polyamines is mediated by transcription factors and not by direct polyamine effects on the promoters of their genes.</p></span></li><li><span>7.</span><span><p>7. Three proteins interacting with the ODC promoter region were found by southwestern blot analysis.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 8","pages":"Pages 991-1001"},"PeriodicalIF":0.0,"publicationDate":"1994-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90070-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19081574","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A comparison of in vitro platinum-DNA adduct formation between carboplatin and cisplatin","authors":"Atsushi Hongo ,&nbsp;Shuji Seki ,&nbsp;Kosuke Akiyama ,&nbsp;Takafumi Kudo","doi":"10.1016/0020-711X(94)90072-8","DOIUrl":"10.1016/0020-711X(94)90072-8","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. DNA damage induced by carboplatin [<em>cis</em>-diammine-(1,1-cyclobutanedi-carboxylato)platinum(II)] was studied <em>in vitro</em> in comparison with cisplatin [<em>cis</em>-diammine-dichloroplatinum(II)]. The drug-induced DNA damage monitored by conformational change of pUC18 plasmid DNA showed that carboplatin required 10 times higher drug concentration and 7.5 times longer incubation time than those of cisplatin to induce the same degree of conformational change on plasmid DNA.</p></span></li><li><span>2.</span><span><p>2. The carboplatin-induced DNA damage was promoted by the increase of pH of the reaction mixture for platinum-DNA adduct formation.</p></span></li><li><span>3.</span><span><p>3. Sequence gel analysis of carboplatin-damaged DNA indicated that carboplatin attacked preferentially the sequence of GG &gt; AG &gt; GA &gt; GNG in the order, similarly to the case of cisplatin.</p></span></li><li><span>4.</span><span><p>4. DNA adducts formed by carboplatin were analyzed by HPLC after a sequential digestion of carboplatin-treated DNA with deoxyribonuclease I and S1 nuclease. A single peak having the same retention time as that of bifunctional adduct of (dGMP)₂Pt(NH₃)₂ appeared by treating DNA with carboplatin. The adduct was assigned to be d(pGpG) &gt; Pt(NH₃)₂.</p></span></li><li><span>5.</span><span><p>5. These results suggested that carboplatin induces the same platinum-DNA adducts as those induced by cisplatin, and that the difference in efficiency or kinetics of DNA damage between carboplatin and cisplatin is due to difference of aquation rate between them.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 8","pages":"Pages 1009-1016"},"PeriodicalIF":0.0,"publicationDate":"1994-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90072-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19081677","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 state of tryptophan-containing sites of human, bovine and rabbit plasminogens with changing solution pHs","authors":"V.N. Nikandrov,&nbsp;G.V. Vorobyova,&nbsp;N.V. Demidchik","doi":"10.1016/0020-711X(94)90076-0","DOIUrl":"10.1016/0020-711X(94)90076-0","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. The state of tryptophan-containing sites is proved to be stable by intrinsic tryptophan fluorescence with pH 5–8, 7–9, and 6–9 in human, rabbit and bovine plasminogen molecules, respectively.</p></span></li><li><span>2.</span><span><p>2. With pH &lt; 5.0 tryptophan-containing sites of human zymogen (in contrast to rabbit and bovine ones) undergo conformational transitions.</p></span></li><li><span>3.</span><span><p>3. With the shift of solution pH from 9 to 12 tryptophan-containing sites of human and rabbit plasminogens are partially disorganized, while tryptophanyls become more available for solvent.</p></span></li><li><span>4.</span><span><p>4. Tryptophan-containing sites of bovine plasminogen molecules are less mobile in structure during changes of solution pH.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 8","pages":"Pages 1043-1047"},"PeriodicalIF":0.0,"publicationDate":"1994-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90076-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19081680","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}