International Journal of Biochemistry最新文献

{"title":"A compendium of reviews in biochemistry and molecular biology published in the second half of 1993","authors":"Ian G Giles","doi":"10.1016/0020-711X(94)90090-6","DOIUrl":"10.1016/0020-711X(94)90090-6","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. A compendium of reviews and mini-reviews in Biochemistry and Molecular Biology published in the second half of 1993 is presented. In all 1063 titles are listed from 127 different publications.</p></span></li><li><span>2.</span><span><p>2. This compendium presents the references Journal by Journal. Keyword and author cross-reference indexes are not included but are available in the computer database that is the companion to this paper version. The electronic form contains details of reviews published since 1990 as listed in this and earlier compendia. Anyone wishing to receive this database should contact the author: it can be distributed either via Internet or on MS-DOS formatted flopppy disks in either <em>Reference Manager</em> or <em>Medline</em> format. Please contact the author for details of the number of pre-formatted floppy disks required.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 10","pages":"Pages 1163-1201"},"PeriodicalIF":0.0,"publicationDate":"1994-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90090-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18851219","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":"Tyrosine protein kinase inhibition and cancer","authors":"Jean A. Boutin","doi":"10.1016/0020-711X(94)90091-4","DOIUrl":"10.1016/0020-711X(94)90091-4","url":null,"abstract":"<div><p>The various aspects of the research on tyrosine protein kinase inhibition and its connections with cancer are presented. The emphasis was made on the theoretical low toxic side effects of specific tyrosine protein kinase inhibitors. Particularly, the strategy of finding peptidic substrate-derived inhibitors or modulators is discussed, with an almost complete compendium of the tyrosine protein kinase peptidic substrates published so far. A series of data has been gathered that may serve as a basis for the discovery of selective and specific tyrosine protein kinase inhibitors by screening on molecular and cellular models. The potential of SH2 domain-interfering agents are also presented as a promising route to new anticancer compounds.</p></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 10","pages":"Pages 1203-1226"},"PeriodicalIF":0.0,"publicationDate":"1994-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90091-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18851220","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":"Molecular mechanism of RNA phage morphogenesis","authors":"P.G. Stock-Ley ,&nbsp;N.J. Stonehouse ,&nbsp;K. Valegård","doi":"10.1016/0020-711X(94)90094-9","DOIUrl":"10.1016/0020-711X(94)90094-9","url":null,"abstract":"<div><p>Recent progress on the molecular mechanism of RNA phage morphogenesis is described. Functional studies, both <em>in vivo</em> and <em>in vitro</em>, are correlated with the latest structural studies on phages, their capsids and the assembly initiation RNA stem-loop.</p></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 10","pages":"Pages 1249-1260"},"PeriodicalIF":0.0,"publicationDate":"1994-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90094-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18851221","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":"Biochemistry and molecular biology of drug-metabolizing sulfotransferase","authors":"Michio Matsui,&nbsp;Hiroshi Homma","doi":"10.1016/0020-711X(94)90093-0","DOIUrl":"10.1016/0020-711X(94)90093-0","url":null,"abstract":"<div><p>Sulfation is an important conjugation reaction in the metabolism of various xenobiotics and endogenous compounds and is catalyzed by sulfotransferase (ST) present in cytosols. The cloning studies on STs have provided the basis for the understanding of the ST multigene family. STs are classified into hydroxysteroid (or alcohol), aryl (or phenol), estrogen, flavonol and polysaccharide STs and recent developments in the molecular characterization of these isoforms are reviewed. Regulation and localization of ST isoforms in various tissues are characterized at the molecular level by virtue of the specific antibodies and the corresponding cDNA probes. The recent developments are summarized. ST inhibitors are potent tools for the study on ST multiplicity and for the characterization of the enzyme structure. It also appears to be important to understand exogenous and endogenous ST inhibitors in clinical environment. The recent developments are reviewed.</p></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 10","pages":"Pages 1237-1247"},"PeriodicalIF":0.0,"publicationDate":"1994-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90093-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18849948","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":"Pancreatic islet hypertrophy in spontaneous maturity onset obese-diabetic CBA/Ca mice","authors":"Carlos D. Figueroa ,&nbsp;Peter V. Taberner","doi":"10.1016/0020-711X(94)90099-X","DOIUrl":"10.1016/0020-711X(94)90099-X","url":null,"abstract":"<div><p>Mature male CBA/Ca mice develop a spontaneous mild diabetes-obesity syndrome which is characterized by hyperglycaemia, hyperinsulinaemia and insulin resistance, and resembles human Type II diabetes mellitus. Immunocytochemical staining of pancreas sections for insulin showed that the pancreas from mature obese mice possessed significantly enlarged islets compared to those from age-matched control (lean) mice. The pancreatic insulin content was significantly greater in 24-week-old obese mice (1.78 ± 0.14mU/mg) compared with lean controls (0.92 ± 0.09 mU/mg). This increase was still apparent at 48 weeks of age. We conclude that, unlike most other rodent models of Type II diabetes, there is no chronic degeneration of beta cells in these mice, so that circulating insulin levels remain high throughout their life. We suggest, therefore, that the male CBA/Ca mouse represents a valuable model for investigating maturity onset diabetes.</p></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 10","pages":"Pages 1299-1303"},"PeriodicalIF":0.0,"publicationDate":"1994-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90099-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18849950","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 exercise on the properties of AMP-deaminase from trout white muscle","authors":"V.I. Lushchak ,&nbsp;K.B. Storey","doi":"10.1016/0020-711X(94)90100-7","DOIUrl":"10.1016/0020-711X(94)90100-7","url":null,"abstract":"<div><p>AMP-deaminase was purified to homogeneity from white skeletal muscle of control (resting) and exercised (1 min burst swimming) rainbow trout, <em>Oncorhynchus mykiss</em>. The enzyme showed a subunit molecular weight of 71,600 ± 550 kD, a <em>K</em>_<em>m</em> AMP of 1.6–1.8 mM at pH 7, and was affected by allosteric inhibitors (GTP, IMP) amd activators (ADP, ATP). AMP-deaminase was inhibited by MgSO₄ but activated by low concentrations of NaCl and KCl (100–150 mM); higher KCl was inhibitory. Exercise resulted in a stable modification of some properties (possibly via reversible phosphorylation); I₅₀ values for IMP decreased by 65% and activation energies (from Arrhenius plots) changed significantly. Other properties were affected by assay pH: <em>K</em>_m AMP decreased by 50% and <em>K</em>_a, ADP decreased by 70% when pH was lowered from pH 7.3 (typical of resting muscle) to pH 6.6 (muscle pH after exhaustive exercise). The data suggest that a stable modification of AMP-deaminase during exercise, coupled with effects of reduced cytosolic pH, could enhance enzyme function in the rapid conversion of AMP to IMP in working fish muscle.</p></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 10","pages":"Pages 1305-1312"},"PeriodicalIF":0.0,"publicationDate":"1994-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90100-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75034860","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":"Net glucose production from acetone in isolated murine hepatocytes. The effect of different pretreatments of mice","authors":"Miklós Péter Kalapos,&nbsp;József Mandl,&nbsp;Gábor Bánhegyi,&nbsp;Ferenc Antoni ,&nbsp;Tamás Garzó","doi":"10.1016/0020-711X(94)90129-5","DOIUrl":"10.1016/0020-711X(94)90129-5","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. To evaluate the condition under which net glucose production from acetone, added as sole substrate, occurs different pretreatments of mice, in combination with starvation, were used; (i) acetone pretreatment (acetone is a known inducer of cytochrome <em>P</em>-450 isozymes involved in this pathway), (ii) fructose pretreatment (to induce NADPH + H⁺ generating enzymes) or (iii) their combination.</p></span></li><li><span>2.</span><span><p>2. There was net glucose formation from acetone only in that case, when the cells were prepared from 48 hr fasted animals pretreated with both acetone and fructose. However, using 2-<em>¹⁴C</em>-acetone, incorporation of <em>¹⁴C</em>-carbon into glucose could be detected in all the cases and, at the same time, acetone was without any effect on protein synthesis.</p></span></li><li><span>3.</span><span><p>3. The addition of acetone increased gluconeogenesis from alanine in almost all the cases. The only exception from this general rule was that the case, when hepatocytes were prepared from acetone pretreated 48 hr starved mice where, instead of the elevation of glucose formation, a decrease of that was caused by acetone.</p></span></li><li><span>4.</span><span><p>4. Acetone decreased ¹⁴C-carbon incorporation into glucose from ¹⁴C-(U)-alanine added at saturating concentration in hepatocytes prepared from starved mice.</p></span></li><li><span>5.</span><span><p>5. Similarly to acetone there was no net glucose formation from acetol either when added alone, however, it enhanced gluconeogenesis from alanine at non-saturating concentrations of the amino acid.</p></span></li><li><span>6.</span><span><p>6. Methylglyoxal proved gluconeogenic in all the cases.</p></span></li><li><span>7.</span><span><p>7. It is concluded that net glucose formation from acetone as sole substrate occurs only under those conditions which are far from a physiological situation, however, when gluconeogenesis from another substrate takes place, acetone can contribute to net glucose formation in hepatocytes prepared from fasted mice.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 9","pages":"Pages 1069-1079"},"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)90129-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18983995","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 methyl methacrylate on mitochondrial function and structure","authors":"Zdzisław Bereznowski","doi":"10.1016/0020-711X(94)90134-1","DOIUrl":"10.1016/0020-711X(94)90134-1","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Treatment of isolated rat liver mitochondria with methyl methacrylate (MM) produced membrane disruption as evidenced by the release of citrate synthase, and changes in the ultrastructure of mitochondria.</p></span></li><li><span>2.</span><span><p>2. At concentration 0.1%, MM uncoupled oxidative phosphorylation as evidenced by stimulation of state 4 respiration supported either by pyruvate plus malate or succinate (+rotenone) and ATP-ase activity in intact mitochondria.</p></span></li><li><span>3.</span><span><p>3. At concentration 1% MM stimulated ATP-ase activity in intact mitochondria and succinate (+rotenone) oxidation at state 4 and was without effect on this substrate oxidation at state 3.</p></span></li><li><span>4.</span><span><p>4. MM inhibited pyruvate plus malate oxidation either at state 3 or in the presence of uncoupling agents.</p></span></li><li><span>5.</span><span><p>5. MM inhibited the NADH oxidase of electron transport particles at a concentration which failed to inhibit either succinic oxidase or the NADH-ferricyanide reductase activity.</p></span></li><li><span>6.</span><span><p>6. The data presented suggest that in the isolated mitochondria MM inhibits NADH oxidation in the vicinity of the rotenone sensitive site of complex I.</p></span></li><li><span>7.</span><span><p>7. The general conclusion is that MM may block an electron transport and to uncouple oxidative phosphorylation in rat liver mitochondria. The overall <em>in vitro</em> effect would be to prevent ATP synthesis which could result in cell death under <em>in vivo</em> conditions.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 9","pages":"Pages 1119-1127"},"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)90134-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18985923","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":"Possible involvement of adenylylation in the modification of a 26 kDa protein in rat parotid acinar cells","authors":"Miki Hara-Yokoyama,&nbsp;Hiroshi Sugiya,&nbsp;Shunsuke Furuyama","doi":"10.1016/0020-711X(94)90132-5","DOIUrl":"10.1016/0020-711X(94)90132-5","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Adenylylation, a posttranslational modification of proteins, was investigated in saponin-permeabilized acinar cells of the rat parotid gland.</p></span></li><li><span>2.</span><span><p>2. When cells were incubated with [2,8-³H]ATP, several proteins, including a 26 kDa protein in the particulate fraction, were labeled.</p></span></li><li><span>3.</span><span><p>3. Upon incubation of cells with [α-³²P]ATP in the presence of cAMP and 3-isobutyl-lmethylxanthine, ³²P-labeling of the 26 kDa protein was observed.</p></span></li><li><span>4.</span><span><p>4. After treatment with snake venom phosphodiesterase, [³²P]AMP was released from the 26kDa protein. Such release was not observed when cells were labeled with [γ-³²P]ATP.</p></span></li><li><span>5.</span><span><p>5. The ³²P-labeling pattern of proteins with [α-³²P]ATP was clearly different from that with [<em>adenylate</em>-³²P]NAD⁺.</p></span></li><li><span>6.</span><span><p>6. The results suggest that the 26 kDa protein is one of the adenylylation substrates in rat parotid acinar cells.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 9","pages":"Pages 1103-1109"},"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)90132-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18534090","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":"Spectral analysis of Fe(III)-complex reduction by hemoglobin: Possible mechanisms of interaction","authors":"John P. Harrington,&nbsp;Rodgers L. Hicks","doi":"10.1016/0020-711X(94)90133-3","DOIUrl":"10.1016/0020-711X(94)90133-3","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Hemoglobin is capable of electron transfer to Fe(III)-complexes of ATP, EDTA, NTA, and citrate leading to formation of reduced Fe(II) and its concurrent release from these chelating compounds as evident in the formation of a Fe(II)-Tris 2,2' bipyridine complex.</p></span></li><li><span>2.</span><span><p>2. Multi-component analysis of kinetic spectra in the visible region (700–500 nm) has permitted a determination of the effect of various chelating molecules bound to Fe(III), pH, the effects of ionic strength, temperature, and the molecular nature of the Fe(III)-complex on reaction rates.</p></span></li><li><span>3.</span><span><p>3. We have examined and compared the reactivities of normal adult hemoglobin A (α₂ β₂) to reduce these Fe(III)-complexes and suggest possible mechanism(s) for the electron transfer process.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 9","pages":"Pages 1111-1117"},"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)90133-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18983998","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}