{"title":"The effect of oxygen on the composition and organisation of the electron transport system of yeast","authors":"D.R. Biggs, Anthony W. Linnane","doi":"10.1016/0006-3002(63)91062-X","DOIUrl":"10.1016/0006-3002(63)91062-X","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 785-788"},"PeriodicalIF":0.0,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91062-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673159","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}
Jacqueline Jollès, Juan Jauregui-Adell, Ida Bernier, Pierre Jollès
{"title":"La structure chimique du lysozyme de blanc d'oeuf de poule: étude détaillée","authors":"Jacqueline Jollès, Juan Jauregui-Adell, Ida Bernier, Pierre Jollès","doi":"10.1016/0006-3002(63)91033-3","DOIUrl":"10.1016/0006-3002(63)91033-3","url":null,"abstract":"<div><p>All the details concerning the establishment of the formula of the chemical structure of hen's egg-white lysozyme (<em>N</em>-acetylmuramide glycanohydrolase, EC 3.2.1.17) (which the authors had briefly indicated in 1961) are reported in the present study. The 18 tryptic units obtained from reduced lysozyme by chromatography on Dowex-1 X2 have beeb joined in the right order thanks to the chymotryptic units containing a basic amino acid and in two instances thanks to the peptic units. The protein is formed by a single polypeptide chain of 129 amino acid residues folded by the 4 bridges of the cystine residues; one of them has already been determined. Some considerations are made on the relations existing between chemical structure and biological activity.</p></div>","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 668-689"},"PeriodicalIF":0.0,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91033-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673340","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 optical rotatory dispersion of myosin a IV. Conformational changes in meromyosins","authors":"Yuji Tonomura , Kazuko Sekiya , Kiichi Imamura","doi":"10.1016/0006-3002(63)91034-5","DOIUrl":"10.1016/0006-3002(63)91034-5","url":null,"abstract":"<div><p>The effect of 8% dioxane on the optical rotatory dispersion of myosin A purified by treatment with DEAE-cellulose was measured in 0.6 M KCl and at pH 7.0 and 20°. The increase in the —<em>b</em><sub>0</sub> term by 5% was followed by a gradual decrease to 0.88 of the original. The —<em>b</em><sub>0</sub> term of L<sub>1</sub>-meromyosin in 0.6 M KCl and at pH 7.0 and 20% was 575 and was unchanged by the addition of dioxane, ATP of PP<sub>1</sub>. On the other hand, the —<em>b</em><sub>0</sub> term of H<sub>2</sub>-meromyosin in 0.3 M KCl and at pH 7.0 and 20% was 263. It increased by several percent immediately after the addition of 8% dioxane and decreased gradually with time. It increased by several percent on the addition of 4 moles <em>p</em>-chloromercuribenzoate, but decreased by several percent on the addition of 8 moles <em>p</em>-chloromercuribenzoate per 10<sup>5</sup> g protein. It was also decreased by the binding of H<sub>2</sub>-meromyosin with F-actin. ATP increased the —<em>b</em><sub>0</sub> term of H<sub>2</sub>-meromyosin by several percent, though PP<sub>1</sub> decreased the term by several percent. Thus these reagents change the helical content of H<sub>2</sub>-meromyosin in ways similar to the case of myosin A. The extents of the changes in the helical content of H<sub>2</sub>-meromyosin by F-actin and ATP were, however, higher than those observed in myosin A.</p></div>","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 690-697"},"PeriodicalIF":0.0,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91034-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673341","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":"Study of [1-14C]glycine incorporation into extractable and residual glycogen of guinea-pig liver in vivo","authors":"Vishwa Nath Singh , T.A. Venkitasubramanian","doi":"10.1016/0006-3002(63)91045-X","DOIUrl":"10.1016/0006-3002(63)91045-X","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 744-746"},"PeriodicalIF":0.0,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91045-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673351","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 effect of insulin on extracellular space and tissue-water content of the isolated rat diaphragm","authors":"G.R. Fritz, E. Knobil","doi":"10.1016/0006-3002(63)91057-6","DOIUrl":"10.1016/0006-3002(63)91057-6","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 773-774"},"PeriodicalIF":0.0,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91057-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673154","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":"Interaction of oestrogen quinones with ethylene diamine","authors":"P.H. Jellinck, Louise Irwin","doi":"10.1016/0006-3002(63)91059-X","DOIUrl":"10.1016/0006-3002(63)91059-X","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 778-780"},"PeriodicalIF":0.0,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91059-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673156","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":"Metabolites of p-aminobenzoic acid III. A metabolic pathway of p-aminobenzoic acid resulting in the sequential formation of p-aminobenzyl alcohol and p-hydroxyaniline","authors":"N.H. Sloane, K.G. Untch, A.W. Johnson","doi":"10.1016/0006-3002(63)91024-2","DOIUrl":"10.1016/0006-3002(63)91024-2","url":null,"abstract":"<div><p>The following sequence of metabolic reactions has been proved by chemical methods to occur in resting cells of acid-fast bacteria: <em>p</em>-aminobenzoic acid → <em>p</em>-aminobenzyl <em>alcohol</em> → <em>p</em>-hydroxyaniline. The first step in this sequence has been demonstrated to be a direct enzymatic reduction by using both ring- and carboxy-<sup>14</sup>C-labeled <em>p</em>-aminobenzoic acid. A synthetic route, which should be of general use, was employed to convert [<sup>14</sup>C]aniline to ring-<sup>14</sup>C-labeled <em>p</em>-aminobenzoic acid. It is suggested that the unique transformation of <em>p</em>-aminobenzyl alcohol to <em>p</em>-hydroxyaniline may be a specific case of a more general mechanism involved in enzymatic hydroxylation of aryl compounds.</p></div>","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 588-593"},"PeriodicalIF":0.0,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91024-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673332","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":"Biosynthèse de l'arginine chez la levure I. Le sort de la Nα-acétylornithine","authors":"R.H. De Deken","doi":"10.1016/0006-3002(63)91026-6","DOIUrl":"10.1016/0006-3002(63)91026-6","url":null,"abstract":"<div><p>An enzyme, transferring the acetyl group of <em>N</em>-<em>α</em>-acetylornithine to the amino group of glutamate, has been demonstrated for <em>Saccharomyces cerevisiae</em>. On the other hand, the enzymic reduction of <em>N</em>-<em>α</em>-acetylglutamate with the formation of <em>N</em>-<em>α</em>-acetyl-glutamic-<em>γ</em>-semialdehyde has been reported previously. The absence of transacetylase in an arginine-requiring mutant (gene <em>ar</em><sub>7</sub>) as well as the above findings prove that: </p><ul><li><span>1.</span><span><p>1. The biosynthesis of ornithine, in yeast, proceeds through acetylated intermediates.</p></span></li><li><span>2.</span><span><p>2. The transacetylase is the only functional pathway for the conversion of <em>N</em>-<em>α</em>-acetylornithine to ornithine, in spite of the simultaneous presence of an <em>N</em>-<em>α</em>-acetylornithinase (<em>N</em>-<em>α</em>-acetylornithine amidohydrolase).</p></span></li></ul><p>At least two steps in the biosynthesis of ornithine are repressible by arginine.</p></div>","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 606-616"},"PeriodicalIF":0.0,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91026-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673334","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":"Changes in free and acetylated amino acids during tobacco mosaic virus multiplication","authors":"Marvin Karasek","doi":"10.1016/0006-3002(63)91030-8","DOIUrl":"10.1016/0006-3002(63)91030-8","url":null,"abstract":"<div><p>Changes in free and acetylated amino acids have been determined in control and infected tobacco plants during logarithmic tobacco mosaic virus multiplication. An increase in free amino acids occurs in infected tissue in the early stages of tobacco mosaic virus synthesis (72 and 144 h) followed by a decrease after 216 h. Acetylamino acids are not present in infected or in normal plant tissue in amounts that exceed 0.2 μmoles per 100 g of plant tissue. The induction of serine acetylase (acetyl-CoA: <span>L</span>-serine <em>N</em>-acetyltransferase) could not be demonstrated during logarithmic tobacco mosaic virus biosynthesis.</p></div>","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 644-648"},"PeriodicalIF":0.0,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91030-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673337","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":"Ascorbic acid-induced fluorescence of a noradrenaline oxidation product","authors":"W.H. Harrison","doi":"10.1016/0006-3002(63)91036-9","DOIUrl":"10.1016/0006-3002(63)91036-9","url":null,"abstract":"<div><p>Ascorbic acid has been found to induce the fluorescence of an intermediate oxidation product of noradrenaline which is formed in a ferricyanide oxidation. The fluorescence of the product is a function of the ascorbic acid and noradrenaline concentration and at conditions at which the fluorescence of the noradrenaline product is optimal the fluorescence of adrenaline, tested similarly, in negligible. The reaction has a definite pH optimum (pH 6) and the fluorescence of the final product depends on the time of the oxidation. The stability and rate of formation of the noradrenaline product is dependent upon the concentration level of the ascorbic acid and ferricyanide. The reaction shows promise as the basis for a new noradrenaline assay.</p></div>","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 705-710"},"PeriodicalIF":0.0,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91036-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673343","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}