The addition of ATP or PPi retarded conspicuously the rate of specific binding of trinitrobenzenesulfonate to one mole of lysine residue in 2.1·105 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 p-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 p-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 p-chloromercuribenzoate and β-mercaptoethanol.
增加ATP或PPi弱智明显的特定绑定trinitrobenzenesulfonate一摩尔的赖氨酸残基105年2.1·克肌凝蛋白A特定绑定的trinitrobenzenesulfonate肌凝蛋白的速度增加4 M LiBr几乎完全融化的螺旋结构肌凝蛋白A率也显著影响肌凝蛋白的治疗与1.5 LiBr灭活的腺苷三磷酸酶(ATP phosphohydrolase,EC 3.6.1.3),而不显著改变整个肌球蛋白A分子的螺旋含量。此外,研究表明,肌球蛋白A经对氯汞苯甲酸盐和β-巯基乙醇处理后重组的肌动球蛋白对高浓度ATP没有清除反应,其ATP酶活性不受底物或EDTA的抑制。加入过量的β-巯基乙醇后,肌球蛋白A中加入的对氯环苯甲醚被完全去除,对氯环苯甲酯和β-巯基乙醇对肌球蛋白A的旋光性影响不显著。
{"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}
Pub Date : 1963-12-13DOI: 10.1016/0006-3002(63)91041-2
D.S.R. Sarma, S. Rajalakshmi, P.S. Sarma
{"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}
Pub Date : 1963-12-13DOI: 10.1016/0006-3002(63)91068-0
Kenzo Tonomura, Fusae Futai, Osamu Tanabe
{"title":"Binding of α-amylase to the cell wall of Aspergillus oryzae","authors":"Kenzo Tonomura, Fusae Futai, Osamu Tanabe","doi":"10.1016/0006-3002(63)91068-0","DOIUrl":"https://doi.org/10.1016/0006-3002(63)91068-0","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 4","pages":"Pages 802-805"},"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)91068-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91956449","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}
Pub Date : 1963-12-13DOI: 10.1016/0006-3002(63)91056-4
Shmuel Razin
{"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}
Pub Date : 1963-12-13DOI: 10.1016/0006-3002(63)91025-4
Wesley C. Starbuck, Harris Busch
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 pK of the respective reacting groups.
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 Nϵ[tris(2-hydroxyethyl)]lysine, since it corresponded to the Nϵ[tris(2-hydroxyethyl)]-lysine, prepared by direct synthesis, with respect to mobility in several chromatographic systems.
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.
{"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}
Pub Date : 1963-12-13DOI: 10.1016/0006-3002(63)91050-3
P.G. Stanley
{"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}
Pub Date : 1963-12-13DOI: 10.1016/0006-3002(63)91033-3
Jacqueline Jollès, Juan Jauregui-Adell, Ida Bernier, Pierre Jollès
All the details concerning the establishment of the formula of the chemical structure of hen's egg-white lysozyme (N-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.
{"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}