International Journal of Biochemistry最新文献

{"title":"In vivo administration of H2 blockers, cimetidine and ranitidine, reduced the contents of the cytochrome P450IID (CYP2D) subfamily and their activities in rat liver microsomes","authors":"Mitsuru Orishiki ,&nbsp;Yoshinori Matsuo ,&nbsp;Mikio Nishioka ,&nbsp;Yoshiyuki Ichikawa","doi":"10.1016/0020-711X(94)90104-X","DOIUrl":"10.1016/0020-711X(94)90104-X","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. The effects of <em>in vivo</em> administration of H₂ blockers, cimetidine and ranitidine (0.6 mmol/kg body weight/day, for 5 days), on several <em>P</em>450 isozymes, the <em>P</em>450IID (CYP2D) subfamily, and their monooxygenase activities in rat liver microsomes were investigated.</p></span></li><li><span>2.</span><span><p>2. <em>In vivo</em> administration of cimetidine and ranitidine decreased the contents of <em>P</em>450 isozymes and the activities of <em>P</em>450-linked monooxygenase systems; i.e., benzphetamine <em>N</em>-demethylase, aminopyrine <em>N</em>-demethylase, 7-ethoxycoumarine <em>O</em>-deethylase, debrisoquine 4-hydroxylase and bufuralol 1'-hydroxylase.</p></span></li><li><span>3.</span><span><p>3. The inhibitory effect on the enzymatic activities of the <em>P</em>450IID (CYP2D)-linked monooxygenase systems was studied by Western blot analysis with serum containing antiCYP2D6 IgG, i.e., LKM1 autoantibody. The amount of <em>P</em>450IID (CYP2D) in liver microsomes decreased more remarkably in the group administered ranitidine or cimetidine <em>in vivo</em> than in controls.</p></span></li><li><span>4.</span><span><p>4. The effects of cimetidine and ranitidine on the activities of the <em>P</em>450IID (CYP2D)-linked monooxygenase systems were investigated <em>in vitro</em>. The activities of debrisoquine 4-hydroxylase and bufuralol 1'-hydroxylase were inhibited <em>in vitro</em> by cimetidine or ranitidine at a higher concentration than that on <em>in vivo</em> administration of either H₂ blocker.</p></span></li><li><span>5.</span><span><p>5. The kinetic parameters for cimetidine or ranitidine as to the activities of debrisoquine 4-hydroxylase and bufuralol 1'-hydroxylase in liver microsomes were determined by means of Lineweaver-Burk plots.</p></span></li><li><span>6.</span><span><p>6. The suppressive effects of cimetidine and ranitidine on the activities of the <em>P</em>450IID (CYP2D)-linked monooxygenase systems <em>in vivo</em> were found to be due to a decrease of the content of the <em>P</em>450IID (CYP2D) protein.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 6","pages":"Pages 751-758"},"PeriodicalIF":0.0,"publicationDate":"1994-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90104-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19056805","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":"Kinetic analysis of reversible closed bicyclic enzyme cascades covering the whole course of the reaction","authors":"R. Varón ,&nbsp;B.H. Havsteen ,&nbsp;M. Molina-Alarcón ,&nbsp;S.E. Szedlacsek ,&nbsp;M. García-Moreno,&nbsp;F. García-Cánovas","doi":"10.1016/0020-711X(94)90108-2","DOIUrl":"10.1016/0020-711X(94)90108-2","url":null,"abstract":"<div><p>A kinetic analysis of the closed bicyclic enzyme cascades is presented. </p><ul><li><span>1.</span><span><p>1. It includes the dependence on time from the onset of the reaction, of the concentration of the modified and unmodified enzyme species involved and the time course equations of the modificational fractions of the interconvertible enzymes.</p></span></li><li><span>2.</span><span><p>2. The transient phase equations obtained allow the definition of new regulatory modification properties.</p></span></li><li><span>3.</span><span><p>3. The expressions for concentrations of the unmodified and modified forms of the interconvertible enzymes, as well as those of the fractional modifications in the steady state are derived as particular cases of the general equations.</p></span></li><li><span>4.</span><span><p>4. These steady state expressions coincide with those obtained by other authors.</p></span></li><li><span>5.</span><span><p>5. The analytical results obtained are discussed in relation to the <em>Escherichia coli</em> glutamine syntethase cascade.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 6","pages":"Pages 787-797"},"PeriodicalIF":0.0,"publicationDate":"1994-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90108-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18911296","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":"Enhancement of self-association of human spectrin by polyethylene glycol","authors":"Nerida Cole,&nbsp;Gregory B. Ralston","doi":"10.1016/0020-711X(94)90109-0","DOIUrl":"10.1016/0020-711X(94)90109-0","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. In the presence of polyethylene glycol, the self-association of human spectrin is enhanced in a manner that depends approx. exponentially on the mass concentration of polyethylene glycol.</p></span></li><li><span>2.</span><span><p>2. For a given mass concentration, the enhancement is independent of the molecular weight of the polyethylene glycol.</p></span></li><li><span>3.</span><span><p>3. These data are consistent with the operation of excluded volume effects, and support the contention that the association of spectrin is likely to be increased in the presence of the high concentration of hemoglobin within the erythrocyte <em>in vivo</em>.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 6","pages":"Pages 799-804"},"PeriodicalIF":0.0,"publicationDate":"1994-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90109-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19056808","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":"Inhibitory activities of partially degraded salivary cystatins","authors":"Satoko Isemura ,&nbsp;Eiichi Saitoh","doi":"10.1016/0020-711X(94)90112-0","DOIUrl":"10.1016/0020-711X(94)90112-0","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Aminoterminally truncated forms of cystatin S and cystatin SN had higher inhibition constants for ficin, but lower ones for cathepsin C (dipeptidyl peptidase I) as compared to their respective full-sized form.</p></span></li><li><span>2.</span><span><p>2. Cystatin SN still retained the inhibitory activity for ficin after reduction and carboxymethylation, although the inhibition constant increased.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 6","pages":"Pages 825-831"},"PeriodicalIF":0.0,"publicationDate":"1994-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90112-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19056809","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 isolation and partial characterization of α1-proteinase inhibitor from the serum of the ostrich (struthio camelus)","authors":"Cheryl R. Kuhn ,&nbsp;Ryno J. Naudé ,&nbsp;James Travis ,&nbsp;Willem Oelofsen","doi":"10.1016/0020-711X(94)90114-7","DOIUrl":"10.1016/0020-711X(94)90114-7","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Native and cleaved α₁-proteinase inhibitor was purified from ostrich serum using Sepharose-blue dextran chromatography, ammonium sulfate precipitation and ion exchange chromatography on DEAE-Toyopearl 650 M at pH 8.8 and 6.5.</p></span></li><li><span>2.</span><span><p>2. Ostrich α₁PI displayed M_r values of 68,100 using gradient PAGE and 66,200 using Ferguson plots.</p></span></li><li><span>3.</span><span><p>3. Isoelectric focusing of ostrich α₁-PI in the pH range 3–10 revealed pi values of 4.84 and 4.91, and in the pH range 4–6 the characteristic microheterogeneity observed for mammalian α₁-PIs was displayed.</p></span></li><li><span>4.</span><span><p>4. The presence of sialic acid, hexoses and hexosamines was detected using chemical methods, but were found in much lower quantities as compared to α₁-PIs of other species.</p></span></li><li><span>5.</span><span><p>5. Western blot analysis demonstrated a positive reaction between the native and cleaved ostrich α₁-PIs and the antibodies to the ostrich α₁-PIs raised in rabbits. No cross-reactivity was demonstrated by Western blot analysis between human α₁-PI and antibodies to ostrich α,-PI.</p></span></li><li><span>6.</span><span><p>6. The inhibitory effect of α₁-PI on elastase and chymotrypsin was also investigated.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 6","pages":"Pages 843-853"},"PeriodicalIF":0.0,"publicationDate":"1994-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90114-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19056675","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":"Anaerobic digestion; modern theory and practice","authors":"","doi":"10.1016/0020-711X(94)90122-8","DOIUrl":"https://doi.org/10.1016/0020-711X(94)90122-8","url":null,"abstract":"","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 6","pages":"Page 856"},"PeriodicalIF":0.0,"publicationDate":"1994-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90122-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91700977","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":"Protein kinases involved in the expression of long-term potentiation","authors":"Tatsuo Suzuki","doi":"10.1016/0020-711X(94)90102-3","DOIUrl":"10.1016/0020-711X(94)90102-3","url":null,"abstract":"<div><p>This review describes the protein kinases that are involved in long-term potentiation (LTP). The following items are described. </p><ul><li><span>1.</span><span><p>1. Ca²⁺/calmodulin-dependent protein kinase II (CaMKII) and protein kinase C (PKC) may play pivotal roles in the different phases of the expression of LTP. This involvement has been indicated mainly by using specific inhibitors of these kinases. The involvement of the CaMKII α-subunit was confirmed in mutant mice which were deficient in the gene for the subunit.</p></span></li><li><span>2.</span><span><p>2. Involvement of persistently active protein kinases in the maintenance of LTP has been proposed and, since then, several studies have focused upon the persistent kinase. Both PKC and CaMKII are possible sources of the persistent kinase activities.</p></span></li><li><span>3.</span><span><p>3. Protein kinases other than CaMKII or PKC (ex. protein kinase A, tyrosine kinases, mitogen-activated kinase) also play roles in the expression of LTP.</p></span></li><li><span>4.</span><span><p>4. Finally, the importance of postsynaptic density as a device where complex chemical reactions related to neuronal signal transduction occur is discussed.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 6","pages":"Pages 735-744"},"PeriodicalIF":0.0,"publicationDate":"1994-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90102-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19056803","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":"Thiol dependent oxidation of enzymes: The last chance against oxidative stress","authors":"A. Del Corso ,&nbsp;M. Cappiello ,&nbsp;U. Mura","doi":"10.1016/0020-711X(94)90103-1","DOIUrl":"10.1016/0020-711X(94)90103-1","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. A survey of known effects of oxidized thiols on enzyme activity reveals a potential concerted action on metabolic pathways determining an impairment of anabolic reduction processes and an activation of the oxidative arm of the hexose monophosphate shunt. Thus it appears that, following oxidative stress, the increase of disulphides may act in restoring a reduced state in the cell by specifically channelling the metabolic energy flux.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 6","pages":"Pages 745-750"},"PeriodicalIF":0.0,"publicationDate":"1994-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90103-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19056804","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":"From molecular biology to therapeutics","authors":"","doi":"10.1016/0020-711X(94)90126-0","DOIUrl":"https://doi.org/10.1016/0020-711X(94)90126-0","url":null,"abstract":"","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 6","pages":"Page 856"},"PeriodicalIF":0.0,"publicationDate":"1994-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90126-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"90021356","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 origins of order; self organization and selection in evolution","authors":"","doi":"10.1016/0020-711X(94)90119-8","DOIUrl":"10.1016/0020-711X(94)90119-8","url":null,"abstract":"","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 6","pages":"Page 855"},"PeriodicalIF":0.0,"publicationDate":"1994-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90119-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"110432232","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}