Pub Date : 1964-11-01DOI: 10.1016/0926-6526(64)90003-5
Lucile Adamson, Sammy Gleason, Constantine Anast
Sulfate incorporation by emryonic chick pelvic rudiments requires protein synthesis.
The incorporation is also dependent on the presence in the incubation medium of both Na+ and K+, and is inhibitable by ouabain.
In the presence of Na+ and K+, the addition of amino acids to the incubation medium stimulates sulfate incorporation. If other monovalent cations are substituted for either Na+ or K+, sulfate incorporation in the absence of amino acids is decreased and stimulation by addition of amino acids is greatly reduced or eliminated.
The possibilities that the Na+ and K+ requirements are due to the participation by these ions in protein synthesis and in transport into the cell of amino acids, sulfate and glucose are discussed.
{"title":"Sulfate incorporation by embryonic chick bone the essentiality of sodium, of potassium, and of protein synthesis","authors":"Lucile Adamson, Sammy Gleason, Constantine Anast","doi":"10.1016/0926-6526(64)90003-5","DOIUrl":"10.1016/0926-6526(64)90003-5","url":null,"abstract":"<div><p>Sulfate incorporation by emryonic chick pelvic rudiments requires protein synthesis.</p><p>The incorporation is also dependent on the presence in the incubation medium of both Na<sup>+</sup> and K<sup>+</sup>, and is inhibitable by ouabain.</p><p>In the presence of Na<sup>+</sup> and K<sup>+</sup>, the addition of amino acids to the incubation medium stimulates sulfate incorporation. If other monovalent cations are substituted for either Na<sup>+</sup> or K<sup>+</sup>, sulfate incorporation in the absence of amino acids is decreased and stimulation by addition of amino acids is greatly reduced or eliminated.</p><p>The possibilities that the Na<sup>+</sup> and K<sup>+</sup> requirements are due to the participation by these ions in protein synthesis and in transport into the cell of amino acids, sulfate and glucose are discussed.</p></div>","PeriodicalId":100172,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Mucoproteins and Mucopolysaccharides","volume":"83 3","pages":"Pages 262-271"},"PeriodicalIF":0.0,"publicationDate":"1964-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6526(64)90003-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23785824","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 : 1964-11-01DOI: 10.1016/0926-6526(64)90020-5
A. Koller, H. Neukom
{"title":"Detection of oligogalacturonic acids by thin-layer chromatography","authors":"A. Koller, H. Neukom","doi":"10.1016/0926-6526(64)90020-5","DOIUrl":"10.1016/0926-6526(64)90020-5","url":null,"abstract":"","PeriodicalId":100172,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Mucoproteins and Mucopolysaccharides","volume":"83 3","pages":"Pages 366-367"},"PeriodicalIF":0.0,"publicationDate":"1964-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6526(64)90020-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23789290","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 : 1964-11-01DOI: 10.1016/0926-6526(64)90022-9
E.R. Berman
{"title":"The biosynthesis of mucopolysaccharides and glycoproteins in pigment epithelial cells of bovine retina","authors":"E.R. Berman","doi":"10.1016/0926-6526(64)90022-9","DOIUrl":"10.1016/0926-6526(64)90022-9","url":null,"abstract":"","PeriodicalId":100172,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Mucoproteins and Mucopolysaccharides","volume":"83 3","pages":"Pages 371-373"},"PeriodicalIF":0.0,"publicationDate":"1964-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6526(64)90022-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23789292","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 : 1964-11-01DOI: 10.1016/0926-6526(64)90024-2
Halina Lis, Nathan Sharon, Ephraim Katchalski
{"title":"Isolation of a mannose-containing glycopeptide from soybean hemagglutinin","authors":"Halina Lis, Nathan Sharon, Ephraim Katchalski","doi":"10.1016/0926-6526(64)90024-2","DOIUrl":"10.1016/0926-6526(64)90024-2","url":null,"abstract":"","PeriodicalId":100172,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Mucoproteins and Mucopolysaccharides","volume":"83 3","pages":"Pages 376-378"},"PeriodicalIF":0.0,"publicationDate":"1964-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6526(64)90024-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23789294","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 : 1964-11-01DOI: 10.1016/0926-6526(64)90019-9
Donald F. Hoelzel Wallach, Miguela V. de Perez Esandi
{"title":"Sialic acid and the electrophoretic mobility of three tumor cell types","authors":"Donald F. Hoelzel Wallach, Miguela V. de Perez Esandi","doi":"10.1016/0926-6526(64)90019-9","DOIUrl":"10.1016/0926-6526(64)90019-9","url":null,"abstract":"","PeriodicalId":100172,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Mucoproteins and Mucopolysaccharides","volume":"83 3","pages":"Pages 363-366"},"PeriodicalIF":0.0,"publicationDate":"1964-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6526(64)90019-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83857167","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 : 1964-11-01DOI: 10.1016/0926-6526(64)90025-4
Spencer Rosenthal, Nathan Sharon
{"title":"The use of Sephadex G-25 for the isolation of nucleotide sugar derivatives from Micrococcus lysodeikticus","authors":"Spencer Rosenthal, Nathan Sharon","doi":"10.1016/0926-6526(64)90025-4","DOIUrl":"10.1016/0926-6526(64)90025-4","url":null,"abstract":"","PeriodicalId":100172,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Mucoproteins and Mucopolysaccharides","volume":"83 3","pages":"Pages 378-380"},"PeriodicalIF":0.0,"publicationDate":"1964-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6526(64)90025-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23789295","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 : 1964-11-01DOI: 10.1016/0926-6526(64)90009-6
J.A Cabezas, J.V Porto, M.D Frois, C Marino, J Arzúa
N-Acetylneuraminic acid has been identified in human tears; other accompanying sialic acids have not been found. N-Acetylneuraminic acid has not been found free, but found. A remarkable release is easily produced by hydrolysis with 0.1 N HCl or 0.1 N H2SO4 at 80° and with neuraminidase (sialidase) (N-acetylneuraminate glycohydrolase, EC 3.2.1.18) at pH 5.5 and 37°, after about 45 min.
Paper electrophoresis shows its main distribution in a fraction of the pherogram with a mobility of −3.8·10−5 cm2 sec−1 V−1 which would correspond to the α-seroglobulins.
The mean concentration in tears is determined, as well as that of hexoses and hexosamines, and a discussion is made about its biochemical signification.
n -乙酰神经氨酸已在人的眼泪中被鉴定出来;其他伴随的唾液酸尚未被发现。n -乙酰神经氨酸不是游离的，而是发现的。用0.1 N HCl或0.1 N H2SO4在80°条件下，用神经氨酸酶(唾液酸酶)(N-乙酰神经氨酸糖水解酶，EC 3.2.1.18)在pH 5.5和37°条件下水解约45分钟，可明显释放α-血清红蛋白。纸电泳显示其主要分布在色谱图的一部分，迁移率为−3.8·10−5 cm2 sec−1 V−1，与α-血清红蛋白相对应。测定了泪液中己糖和己糖胺的平均浓度，并讨论了其生化意义。
{"title":"Acide sialique dans les larmes humaines","authors":"J.A Cabezas, J.V Porto, M.D Frois, C Marino, J Arzúa","doi":"10.1016/0926-6526(64)90009-6","DOIUrl":"10.1016/0926-6526(64)90009-6","url":null,"abstract":"<div><p><em>N</em>-Acetylneuraminic acid has been identified in human tears; other accompanying sialic acids have not been found. <em>N</em>-Acetylneuraminic acid has not been found free, but found. A remarkable release is easily produced by hydrolysis with 0.1 N HCl or 0.1 N H<sub>2</sub>SO<sub>4</sub> at 80° and with neuraminidase (sialidase) (<em>N</em>-acetylneuraminate glycohydrolase, EC 3.2.1.18) at pH 5.5 and 37°, after about 45 min.</p><p>Paper electrophoresis shows its main distribution in a fraction of the pherogram with a mobility of −3.8·10<sup>−5</sup> cm<sup>2</sup> sec<sup>−1</sup> V<sup>−1</sup> which would correspond to the α-seroglobulins.</p><p>The mean concentration in tears is determined, as well as that of hexoses and hexosamines, and a discussion is made about its biochemical signification.</p></div>","PeriodicalId":100172,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Mucoproteins and Mucopolysaccharides","volume":"83 3","pages":"Pages 318-325"},"PeriodicalIF":0.0,"publicationDate":"1964-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6526(64)90009-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91068623","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 : 1964-11-01DOI: 10.1016/0926-6526(64)90012-6
A Morawiecki
In alkyl sulfate detergents the M- and N-group antigen mucoproteins having a molecular weight of about 106 Daltons dissociate into subunits. Their molecular weight at infinite dilution was determined as 3·104 Daltons. At finite mucoprotein concentrations a dynamic association-dissociation equilibrium between the subunits was observed. On dissolving in dimethylformamide-formic acid mixture (9:1 v/v), the M and N mucoprotein macromolecules disintegrated into fragments with a molecular weight of about 9·104 Daltons. Removal of the detergent from the dissociated mucoprotein resulted in reaggregation of the subunits, and the material exhibited unchanged serological activity. The observations suggest that in water solutions the subunits are kept in aggressive forms by hydrophobic bonds. This may be caused by asymmetric distribution of hydrophilic residues (sugars, amino sugars, and sialic acid) along the polypeptide backbone of the subunits.
{"title":"Dissociation of M- and N-group mucoproteins in subunits in detergen solutions","authors":"A Morawiecki","doi":"10.1016/0926-6526(64)90012-6","DOIUrl":"10.1016/0926-6526(64)90012-6","url":null,"abstract":"<div><p>In alkyl sulfate detergents the M- and N-group antigen mucoproteins having a molecular weight of about 10<sup>6</sup> Daltons dissociate into subunits. Their molecular weight at infinite dilution was determined as 3·10<sup>4</sup> Daltons. At finite mucoprotein concentrations a dynamic association-dissociation equilibrium between the subunits was observed. On dissolving in dimethylformamide-formic acid mixture (9:1 v/v), the M and N mucoprotein macromolecules disintegrated into fragments with a molecular weight of about 9·10<sup>4</sup> Daltons. Removal of the detergent from the dissociated mucoprotein resulted in reaggregation of the subunits, and the material exhibited unchanged serological activity. The observations suggest that in water solutions the subunits are kept in aggressive forms by hydrophobic bonds. This may be caused by asymmetric distribution of hydrophilic residues (sugars, amino sugars, and sialic acid) along the polypeptide backbone of the subunits.</p></div>","PeriodicalId":100172,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Mucoproteins and Mucopolysaccharides","volume":"83 3","pages":"Pages 339-347"},"PeriodicalIF":0.0,"publicationDate":"1964-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6526(64)90012-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23785833","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 : 1964-11-01DOI: 10.1016/0926-6526(64)90004-7
Grant H. Barlow, Lyle J. Coen, Milton M. Mozen
Since improvements in the isolation procedure have resulted in heparin of high biological activity, the question of species difference has been reexamined. We have isolated heparin from dog, beef, hog, sheep and human tissue by selective fractionation with quaternary ammonium compounds. Based on our results we would suggest that heparins isolated from various mammalian species are biologically, chemically and physically similar. The biological variations previously observed may well be a result of different degree of purity in the heparin isolated.
{"title":"A biological chemical and physical comparison of heparin from differential mammalian species","authors":"Grant H. Barlow, Lyle J. Coen, Milton M. Mozen","doi":"10.1016/0926-6526(64)90004-7","DOIUrl":"10.1016/0926-6526(64)90004-7","url":null,"abstract":"<div><p>Since improvements in the isolation procedure have resulted in heparin of high biological activity, the question of species difference has been reexamined. We have isolated heparin from dog, beef, hog, sheep and human tissue by selective fractionation with quaternary ammonium compounds. Based on our results we would suggest that heparins isolated from various mammalian species are biologically, chemically and physically similar. The biological variations previously observed may well be a result of different degree of purity in the heparin isolated.</p></div>","PeriodicalId":100172,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Mucoproteins and Mucopolysaccharides","volume":"83 3","pages":"Pages 272-277"},"PeriodicalIF":0.0,"publicationDate":"1964-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6526(64)90004-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23785825","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}
扫码关注我们
求助内容：
应助结果提醒方式：
京公网安备 11010802042870号