Karamba J. Ceesay, Lynn R. Rider, Lawrence W. Bergman , Martin T. Tuck
{"title":"The relationship between the trimethylation of lysine 77 and cytochrome c metabolism in Saccharomyces cerevisiae","authors":"Karamba J. Ceesay, Lynn R. Rider, Lawrence W. Bergman , Martin T. Tuck","doi":"10.1016/0020-711X(94)90172-4","DOIUrl":"10.1016/0020-711X(94)90172-4","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Site directed mutations were constructed in the yeast iso-1-cytochrome <em>c</em> gene adjacent to the lysine 77 (methylation site) codon.</p></span></li><li><span>2.</span><span><p>2. These mutant genes were then cloned and transformed into the <em>S. cerevisiae</em> strain B-6642 which contains a deficiency in the iso-1-cytochrome <em>c</em> gene.</p></span></li><li><span>3.</span><span><p>3. The resulting transformants were screened for cytochrome <em>c</em> production using gel electrophoresis.</p></span></li><li><span>4.</span><span><p>4. Amino acid analysis of the mutated cytochromes <em>c</em> demonstrated varying levels of trimethyllysine formation, depending on the nature of the site directed mutation.</p></span></li><li><span>5.</span><span><p>5. The resulting transformants were then used as tools in order to investigate the relationship between trimethyllysine formation and various aspects of cytochrome <em>c</em> metabolism including protein stability and heme conjugation.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 5","pages":"Pages 721-734"},"PeriodicalIF":0.0,"publicationDate":"1994-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90172-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19004218","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":"Ependymins and their potential role in neuroplasticity and regeneration: Calcium-binding meningeal glycoproteins of the cerebrospinal fluid and extracellular matrix","authors":"Werner Hoffmann","doi":"10.1016/0020-711X(94)90160-0","DOIUrl":"10.1016/0020-711X(94)90160-0","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Ependymins are unique, highly divergent secretory proteins of the fish endomeninx. Thus far, no homologous sequences have been characterized in mammals.</p></span></li><li><span>2.</span><span><p>2. Soluble ependymins are the predominant constituents of the cerebrospinal fluid of many teleost fish. A bound form of these glycoproteins is associated with the extracellular matrix probably with collagen fibrils. The latter may be the functional form of ependymins.</p></span></li><li><span>3.</span><span><p>3. Ependymins bind Ca<sup>2+</sup> via N-linked sialic acid residues leading to a conformational transition.</p></span></li><li><span>4.</span><span><p>4. The molecular function of ependymins seems to be related to cell contact phenomena involving the extracellular matrix. For example, adhesive or anti-adhesive interactions may possibly influence ingrowing axons.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 5","pages":"Pages 607-619"},"PeriodicalIF":0.0,"publicationDate":"1994-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90160-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18998521","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":"Kinetics of manganese reconstitution and thiol group exposition in dialyzed rat mammary gland arginase","authors":"J.M. Fuentes, M.L. Campo, G. Soler","doi":"10.1016/0020-711X(94)90165-1","DOIUrl":"10.1016/0020-711X(94)90165-1","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Rat mammary gland arginase is a metallo-enzyme dependent on Mn<sup>2 +</sup>, which can be only partially substituted by Cd<sup>2 +</sup>.</p></span></li><li><span>2.</span><span><p>2. Reconstitution of the activity of dialyzed arginase by manganese is a two-phase process; the second phase is independent of the cation concentration, with a half-time recovery (<em>t</em><span><math><mtext>1</mtext><mtext>2</mtext></math></span>) of 10.77 min.</p></span></li><li><span>3.</span><span><p>3. The apparent K<sub>m</sub> for Mn<sup>2+</sup> is 280 μ M and 10.5 μ M for enzyme dialyzed for 24 and 72 hr, respectively.</p></span></li><li><span>4.</span><span><p>4. Treatment with 5 mM EDTA at pH 6 totally inhibits enzyme activity, which is reconstituted by Mn<sup>2+</sup>.</p></span></li><li><span>5.</span><span><p>5. Results obtained with iodocetamide treatment suggest the existence of sulphydryl groups accessible only when the enzyme is dialyzed.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 5","pages":"Pages 653-659"},"PeriodicalIF":0.0,"publicationDate":"1994-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90165-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18998525","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":"Binding of meso-tetra(4-sulfonatophenyl)porphine to haemopexin and albumin studied by spectroscopy methods","authors":"J. Bartošová, I. Kalousek, Z. Hrkal","doi":"10.1016/0020-711X(94)90162-7","DOIUrl":"10.1016/0020-711X(94)90162-7","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. The interaction of haemopexin and albumin with TPPS<sub>4</sub> was studied by measuring the absorption and fluorescence spectra. Haemopexin was found to have one strong TPPS<sub>4</sub> binding center (<em>K</em><sub><em>a</em></sub> = 3 × 10<sup>7</sup><em>M</em><sup>−1</sup>).</p></span></li><li><span>2.</span><span><p>2. Haem-haemopexin complex appears to have no specific binding site for TPPS<sub>4</sub>. Occupation of the specific binding center of haemopexin molecule by a haem abolishes TPPS<sub>4</sub> binding.</p></span></li><li><span>3.</span><span><p>3. Albumin was found to possess one strong TPPS<sub>4</sub> binding center (K<sub>a</sub> = 3 × 10<sup>6</sup>M<sup>−1</sup>) besides two or three weak binding sites (<em>K</em><sub><em>a</em></sub> = 2 × 10<sup>5</sup><em>M</em><sup>−1</sup>).</p></span></li><li><span>4.</span><span><p>4. Haern-albumin complex possesses only one weak TPPS<sub>4</sub> binding site (<em>K</em><sub><em>a</em></sub> = 7 × <em>l</em><em>O</em><sup>5</sup><em>M</em><sup>−1</sup>). These observations suggest identity of primary binding sites of TPPS<sub>4</sub> and haem on albumin molecule.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 5","pages":"Pages 631-637"},"PeriodicalIF":0.0,"publicationDate":"1994-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90162-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18998523","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}
Harvey N. Rubin, Randy S. Stefanko , Mostafa N. Halim
{"title":"Evidence that the 5' end of rabbit globin mRNA is hybridized with its 3' end","authors":"Harvey N. Rubin, Randy S. Stefanko , Mostafa N. Halim","doi":"10.1016/0020-711X(94)90170-8","DOIUrl":"10.1016/0020-711X(94)90170-8","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. A radiopolyadenylated rabbit globin mRNA was treated with different concentrations of ribonuclease V<sub>1</sub> from cobra venom.</p></span></li><li><span>2.</span><span><p>2. The enzymatic digests were chromatographed on an aminophenylboronate-agarose column, which specifically captured the cap structure i.e. n<sup>7</sup>G(5') ppp (5') NmP.</p></span></li><li><span>3.</span><span><p>3. When the capture fragment was chromatographed on a Sephadex G-100 column, its size was smaller than the native molecule and also bore radioactivity, i.e. a poly(A) tail.</p></span></li><li><span>4.</span><span><p>4. These results provide evidence that the 5' end (which encompasses the cap structure) of rabbit globin mRNA is hybridized and in close proximity to its 3' end.</p></span></li><li><span>5.</span><span><p>5. We conclude that this conformation is required for messenger translation efficiency.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 5","pages":"Pages 703-710"},"PeriodicalIF":0.0,"publicationDate":"1994-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90170-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19004216","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}
P. Chiodi , B. Clani , S. Kentroti , F. Maccari , A. Vernadakis , L. Angelucci , M.T. Ramacci
{"title":"Carnitine and derivatives in the central nervous system of chick embryo","authors":"P. Chiodi , B. Clani , S. Kentroti , F. Maccari , A. Vernadakis , L. Angelucci , M.T. Ramacci","doi":"10.1016/0020-711X(94)90171-6","DOIUrl":"10.1016/0020-711X(94)90171-6","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Carnitine contents and the activity of carnitine acetyltransferase in the egg, in the embryo, and in different brain areas of central nervous system in chick embryo were determined in the course of development.</p></span></li><li><span>2.</span><span><p>2. The egg showed low levels of free carnitine and acetylcarnitine.</p></span></li><li><span>3.</span><span><p>3. In the whole embryo, at first stages of development, long chain acylcarnitines and acetylcarnitine were the best represented classes of carnitines.</p></span></li><li><span>4.</span><span><p>4. In the brain regions acetylcarnitine levels, high at the first days, showed a continual decrease during development.</p></span></li><li><span>5.</span><span><p>5. The activity of carrietine acetyltransferase increased and was totally related to development.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 5","pages":"Pages 711-720"},"PeriodicalIF":0.0,"publicationDate":"1994-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90171-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19004217","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":"Prostaglandin E2/parathyroid hormone-induced suppression of alkaline phosphatase activity is mediated by protein kinase C","authors":"Tsuneo Miya , Masatoshi Tagawa , Noriko Kato , Kikuo Takahashi , Kenichi Sato , Shinji Fujimura","doi":"10.1016/0020-711X(94)90163-5","DOIUrl":"10.1016/0020-711X(94)90163-5","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Bone resorptive factors, prostaglandin E2 and parathyroid hormone are shown to suppress alkaline phosphatase activity in a rat osteoblastic cell line.</p></span></li><li><span>2.</span><span><p>2. Phorbol myristate acetate, but not dibutyryl cAMP or calcium ionophore can suppress alkaline phosphatase activity.</p></span></li><li><span>3.</span><span><p>3. The protein kinase C inhibitors (H89, staurosporine) are able to block the suppression of alkaline phosphatase activity induced by prostaglandin E2 and parathyroid hormone.</p></span></li><li><span>4.</span><span><p>4. These data suggest that protein kinase C is involved in the inhibition of alkaline phosphatase activity induced by prostaglandin E2 and parathyroid hormone.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 5","pages":"Pages 639-643"},"PeriodicalIF":0.0,"publicationDate":"1994-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90163-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18998524","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":"Thrombin induces S-d-lactoylglutathione accumulation by enhancing platelet glycolytic pathway","authors":"Giuliana Leoncini, Enrica Buzzi","doi":"10.1016/0020-711X(94)90166-X","DOIUrl":"10.1016/0020-711X(94)90166-X","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Thrombin addition to human platelets stimulates <span>l</span>(+)lactate formation and S-D-lactoylglutathione (SDL) accumulation.</p></span></li><li><span>2.</span><span><p>2. Monoiodoacetamide decreases lactate formation and potentiates SDL accumulation through a significant increase of dihydroxyacetone phosphate and fructose 1,6bisphosphate intracellular levels both in resting and in activated platelets.</p></span></li><li><span>3.</span><span><p>3. A similar effect is produced by exogenous methylglyoxal on L(+)lactate formation and SDL accumulation.</p></span></li><li><span>4.</span><span><p>4. Resting platelets completely transform (1 hr at 37°C) the ketoaldehyde into <span>d</span>(-)lactate:</p></span></li><li><span>5.</span><span><p>5. When platelets are incubated in the presence of thrombin only 60% of the ketoaldehyde is found as <span>d</span>(-)lactate and the accumulated S-<span>d</span>-lactoylglutathione represents about the 0.7% of the initial substrate.</p></span></li><li><span>6.</span><span><p>6. During platelet stimulation with thrombin the hemithioacetal adduct, formed as a by-product of glycolytic pathway, can be rapidly removed for important steps of cellular activation.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 5","pages":"Pages 661-665"},"PeriodicalIF":0.0,"publicationDate":"1994-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90166-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19004212","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}
Willy J. Malaisse , Monique Blesemans , Rudolph Willem
{"title":"Generation of C3- and C2-deuterated l-lactic acid by human erythrocytes exposed to d-[1-13C]glucose, d-[2-13c]glucose and d-[6-13C]glucose in the presence of D2O","authors":"Willy J. Malaisse , Monique Blesemans , Rudolph Willem","doi":"10.1016/0020-711X(94)90169-4","DOIUrl":"10.1016/0020-711X(94)90169-4","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. The generation of C<sub>2</sub>- and C<sub>3</sub>-deuterated <span>l</span>-lactate was monitored by <sup>13</sup>C NMR in human erythrocytes exposed to <span>d</span>-[1-<sup>13</sup>glucose, <span>d</span>-[2-<sup>13</sup>C]glucose or <span>d</span>-te-<sup>13</sup>C]glucose and incubated in a medium prepared in D<sub>2</sub>O.</p></span></li><li><span>2.</span><span><p>2. The results suggested that the deuteration of the C<sub>1</sub> of <span>d</span>-fructose 6-phosphate in the phosphoglucoisomerase reaction, the deuteration of the C<sub>1</sub> of <span>d</span>-glyceraldehyde-3-phosphate in the sequence of reactions catalyzed by triose phosphate isomerase and aldolase and the deuteration of the C<sub>3</sub> of pyruvate in the reaction catalyzed by pyruvate kinase were all lower than expected from equilibration with D<sub>2</sub>O.</p></span></li><li><span>3.</span><span><p>3. Moreover, about 40% of the molecules of pyruvate generated by glycolysis apparently underwent deuteration on their C<sub>3</sub> during interconversion of the 2-keto acid and <span>l</span>-alanine in the reaction catalyzed by glutamate-pyruvate transaminase.</p></span></li><li><span>4.</span><span><p>4. The occurrence of the latter process was also documented in cells exposed to exogenous [3-<sup>13</sup>C]pyruvate.</p></span></li><li><span>5.</span><span><p>5. This methodological approach is proposed to provide a new tool to assess in intact cells the extent of back-and-forth interconversion of selected metabolic intermediates.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 5","pages":"Pages 697-702"},"PeriodicalIF":0.0,"publicationDate":"1994-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90169-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19004215","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":"Multiplicity of dog kidney high-Km aldose reductase and conversion mechanism into aldose reductase","authors":"Miyako Ohta, Tsuyoshi Tanimoto, Takao Hayakawa","doi":"10.1016/0020-711X(94)90015-9","DOIUrl":"10.1016/0020-711X(94)90015-9","url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. High-<em>K</em><sub><em>m</em></sub>, aldose reductase purified from dog kidney inner medulla was easily converted into aldose reductase by incubation in the neutral buffer solution.</p></span></li><li><span>2.</span><span><p>2. High-<em>K</em><sub><em>m</em></sub>, aldose reductase was found to be in multiple forms, and was separated into three kinds of species designated as a-, b- and c-forms by HPLC.</p></span></li><li><span>3.</span><span><p>3. The a-form observed as a single peak by HPLC was assumed to be present in three forms (al-, a2- and a3-forms), one was aldose reductase (a 1-form) and the others were the precursors of aldose reductase (a2- and a3-form).</p></span></li><li><span>4.</span><span><p>4. The b-form was rapidly converted into the a3-form, followed slowly by the a2-form and finally into the a 1-form.</p></span></li><li><span>5.</span><span><p>5. The c-form was either directly converted into the al-form, or indirectly into the a2-form followed by the al-form.</p></span></li><li><span>6.</span><span><p>6. Four kinds of species (a2-, a3-, b- and c-forms) of high-Ap, aldose reductase were finally converted into aldose reductase (al-form).</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 4","pages":"Pages 565-573"},"PeriodicalIF":0.0,"publicationDate":"1994-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90015-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19011692","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}