{"title":"On the active site of myosin A-adenosine triphosphatase IV. Properties of binding of trinitrobenzenesulfonate and p-chloromercuribenzoate to myosin a","authors":"Yuji Tonomura , Junko Yoshimura, Toshiyuki Ohnishi","doi":"10.1016/0006-3002(63)91035-7","DOIUrl":"10.1016/0006-3002(63)91035-7","url":null,"abstract":"<div><p>The addition of ATP or PP<sub>i</sub> retarded conspicuously the rate of specific binding of trinitrobenzenesulfonate to one mole of lysine residue in 2.1·10<sup>5</sup> g of myosin A. The rate of specific binding of trinitrobenzenesulfonate to myosin A was increased in 4M LiBr which melts almost completely the helical structure of myosin A. The rate was also remarkably influenced by the treatment of myosin A with 1.5 M LiBr which inactivated ATPase (ATP phosphohydrolase, EC 3.6.1.3) without changing significantly the helical content of the myosin A molecule as a whole. Furthermore, it was demonstrated that actomyosin reconstituted from myosin A treated with <em>p</em>-chloromercuribenzoate and β-mercaptoethanol does not show a clearing response on addition of high concentrations of ATP and its ATPase activity is not inhibited by the substrate or by EDTA. The <em>p</em>-chloromercuribenzotae added was completely removed from myosin A by the further addition of excess β-mercaptoethanol and the optical rotatory dispersion of myosin A was insignificantly altered by the treatment with <em>p</em>-chloromercuribenzoate and β-mercaptoethanol.</p></div>","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 698-704"},"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)91035-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673342","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":"Studies on the reaction between nicotinamide and iodoacetic acid","authors":"D.S.R. Sarma, S. Rajalakshmi, P.S. Sarma","doi":"10.1016/0006-3002(63)91041-2","DOIUrl":"10.1016/0006-3002(63)91041-2","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 733-736"},"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)91041-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673347","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":"Abnormal human hemoglobins IX. Chemistry of hemoglobin JBaltimore","authors":"Corrado Baglioni , David J. Weatherall","doi":"10.1016/0006-3002(63)91029-1","DOIUrl":"10.1016/0006-3002(63)91029-1","url":null,"abstract":"<div><p>A human abnormal hemoglobin with the electrophoretic mobility of hemoglobin J has been isolated and studied. The amino acid substitution in this abnormal hemoglobin has been investigated. It has been found that an aspartic acid residue substitutes in this hemoglobin J the glycine residue present in position 16 of the β peptide chain. There are reasons to believe that the hemoglobin J studied is different from other hemoglobin J's. Accordingly, the hemoglobin studied has been specifically designated hemoglobin J<sub>Baltimore</sub>.</p></div>","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 637-643"},"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)91029-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23676018","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 control of respiration in brain slices","authors":"Shigeki Minakami, Katsuko Kakinuma, Haruhisa Yoshikawa","doi":"10.1016/0006-3002(63)91070-9","DOIUrl":"10.1016/0006-3002(63)91070-9","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 808-811"},"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)91070-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673168","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":"Incomplete separation of human thyroglobulin from serum proteins by chromatography on diethylaminoethyl cellulose","authors":"P.G. Stanley","doi":"10.1016/0006-3002(63)91050-3","DOIUrl":"10.1016/0006-3002(63)91050-3","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 756-758"},"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)91050-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673147","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 nystatin by mycoplasma (pleuropneumonia-like organisms)","authors":"Shmuel Razin","doi":"10.1016/0006-3002(63)91056-4","DOIUrl":"10.1016/0006-3002(63)91056-4","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 771-773"},"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)91056-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673153","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":"Hydroxyethylation of amino acids in plasma albumin with ethylene oxide","authors":"Wesley C. Starbuck, Harris Busch","doi":"10.1016/0006-3002(63)91025-4","DOIUrl":"10.1016/0006-3002(63)91025-4","url":null,"abstract":"<div><p>The reaction of ethylene oxide with amino acids in bovine plasma albumin was studied under various conditions of pH and time. Ethylene oxide reacted with arginyl, cystyl, histidyl, lysyl, methionyl and tyrosyl residues in albumin. The maximal reaction of arginyl, histidyl, lysyl and tyrosyl residues occurred at pH values equal to or greater than the p<em>K</em> of the respective reacting groups.</p><p>The reaction of ethylene oxide with the above amino acid residues resulted in the formation of 21 new peaks detected by chromatograpic analysis of the amino acids. The amino acids from which most of these products originated were detected by labeling the albumin biosynthetically with individual radioactive amino acids before hydroxyethylation. The major product of hydroxyethylation of lysine was apparently <em>Nϵ</em>[tris(2-hydroxyethyl)]lysine, since it corresponded to the <em>Nϵ</em>[tris(2-hydroxyethyl)]-lysine, prepared by direct synthesis, with respect to mobility in several chromatographic systems.</p><p>The accessibility of some lysyl and methionyl residues in albumin to ethylene oxide may be dependent upon a partial change in the tertiary structure of albumin, resulting from the reaction of cystyl residues in albumin with ethylene oxide.</p></div>","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 594-605"},"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)91025-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23673333","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}