Pub Date : 1963-11-15DOI: 10.1016/0006-3002(63)90903-X
R.K. Bretthauer , D.R. Wilken , R.G. Hansen
The biosynthesis of phosphomannan by cultures of Hansenula holstii NRRL Y-2448 has been demonstrated to proceed from glucose with all carbons remaining intact. Enzymes were found in cell-free extracts capable of converting glucose to guanosine diphosphate mannose via mannose 1-phosphate. The isomerization of glucose to mannose occured as hexose phosphate and not as nucleotide hexose. The isolation and identification of guanosine diphosphate mannose from perchloric acid extracts gave further evidence for the proposal that guanosine diphosphate mannose is a precursor of phosphomannan.
{"title":"The biosynthesis of guanosine diphosphate mannose and phosphomannan by Hansanula holstii","authors":"R.K. Bretthauer , D.R. Wilken , R.G. Hansen","doi":"10.1016/0006-3002(63)90903-X","DOIUrl":"10.1016/0006-3002(63)90903-X","url":null,"abstract":"<div><p>The biosynthesis of phosphomannan by cultures of <em>Hansenula holstii</em> NRRL Y-2448 has been demonstrated to proceed from glucose with all carbons remaining intact. Enzymes were found in cell-free extracts capable of converting glucose to guanosine diphosphate mannose <em>via</em> mannose 1-phosphate. The isomerization of glucose to mannose occured as hexose phosphate and not as nucleotide hexose. The isolation and identification of guanosine diphosphate mannose from perchloric acid extracts gave further evidence for the proposal that guanosine diphosphate mannose is a precursor of phosphomannan.</p></div>","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 3","pages":"Pages 420-429"},"PeriodicalIF":0.0,"publicationDate":"1963-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)90903-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23670741","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 : 1963-11-15DOI: 10.1016/0006-3002(63)90928-4
Philipp Strittmatter , Helen B. Burch
{"title":"The heme protein in ganglia of Spisula solidissima","authors":"Philipp Strittmatter , Helen B. Burch","doi":"10.1016/0006-3002(63)90928-4","DOIUrl":"10.1016/0006-3002(63)90928-4","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 3","pages":"Pages 562-563"},"PeriodicalIF":0.0,"publicationDate":"1963-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)90928-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23675998","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 : 1963-11-15DOI: 10.1016/0006-3002(63)90901-6
Donald G. Cochran
Mitochondria isolated from cockroach thoracic muscles have been used to demonstrate that the rate of oxidation of several Krebs-cycle intermediates is under the control of adenosine diphosphate concentration. Respiratory-control indices as high as 25 have been achieved with both pyruvate and glutamate. Contrarily, the rate of oxidation of α-glycerol phosphate is influenced by adenosine diphosphate concentration to only a minor degree, but is markedly inhibited by accumulation of the oxidation product. When the ratio [reactant]/[product] is approx. 3, oxidation of α-glycerol phosphate becomes very low. These findings are used to propose a theory which may satisfactorily explain the problem of respiratory control in insect muscles.
{"title":"Respiratory control in cockroach-muscle mitochondria","authors":"Donald G. Cochran","doi":"10.1016/0006-3002(63)90901-6","DOIUrl":"10.1016/0006-3002(63)90901-6","url":null,"abstract":"<div><p>Mitochondria isolated from cockroach thoracic muscles have been used to demonstrate that the rate of oxidation of several Krebs-cycle intermediates is under the control of adenosine diphosphate concentration. Respiratory-control indices as high as 25 have been achieved with both pyruvate and glutamate. Contrarily, the rate of oxidation of α-glycerol phosphate is influenced by adenosine diphosphate concentration to only a minor degree, but is markedly inhibited by accumulation of the oxidation product. When the ratio [reactant]/[product] is approx. 3, oxidation of α-glycerol phosphate becomes very low. These findings are used to propose a theory which may satisfactorily explain the problem of respiratory control in insect muscles.</p></div>","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 3","pages":"Pages 393-403"},"PeriodicalIF":0.0,"publicationDate":"1963-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)90901-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23670739","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 : 1963-11-15DOI: 10.1016/0006-3002(63)90917-X
Lester Packer, Eugene Corriden, Reginald H. Marchant
{"title":"Coupling of energy to mitochondrial swelling","authors":"Lester Packer, Eugene Corriden, Reginald H. Marchant","doi":"10.1016/0006-3002(63)90917-X","DOIUrl":"10.1016/0006-3002(63)90917-X","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 3","pages":"Pages 534-536"},"PeriodicalIF":0.0,"publicationDate":"1963-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)90917-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23672493","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 : 1963-11-15DOI: 10.1016/0006-3002(63)90904-1
E. Eggermont
A suspension of epithelial cells of the human tongue has been shown to form glycogen and CO2 from glucose, fructose, maltose and sucrose. Carbon 1 of glucose is converted to CO2 much more rapidly than carbon 6.
{"title":"Le métabolisme des cellules épithéliales de la langue chez l'homme","authors":"E. Eggermont","doi":"10.1016/0006-3002(63)90904-1","DOIUrl":"10.1016/0006-3002(63)90904-1","url":null,"abstract":"<div><p>A suspension of epithelial cells of the human tongue has been shown to form glycogen and CO<sub>2</sub> from glucose, fructose, maltose and sucrose. Carbon 1 of glucose is converted to CO<sub>2</sub> much more rapidly than carbon 6.</p></div>","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 3","pages":"Pages 430-436"},"PeriodicalIF":0.0,"publicationDate":"1963-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)90904-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23670742","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 : 1963-11-15DOI: 10.1016/0006-3002(63)90912-0
H. Hagihira, T.H. Wilson, E.C.C. Lin
The properties of the glucose-transport system of Escherichia coli K10 were studied by following intracellular accumulation of 14C-labeled α-methylglucoside. A mutant defective in the uptake of glucose was found to be unable to accumulate α-methylglucoside to a significant level, confirming the view that the carrier for glucose also acts on α-methylglucoside. Although the glucoside was not incorporated into cellular constituents or metabolized for energy, about one-half of the accumulated molecules underwent phosphorylation while one-half remained as the free glucoside. Studies on the inhibition of uptake of the glucoside showed that the affinity of the compound depended upon the substituents on C-2, C-3 and C-6. Structural modifications at C-1, on the other hand, had relatively little effect on the affinity unless a large aglycone was added. α-Methylglucoside accumulated by the cells was gradually lost upon dilution of the cells in simple inorganic medium. The rate of exit could be accelerated by two groups of compounds: non-metabolizable structural analogs with affinity for the transport carrier and metabolizable compounds which entered the cell by other routes. The effect of the latter group depended upon their further metabolism within the cell rather than their own direct effects on the carrier system.
{"title":"Studies on the glucose-transport system in Escherichia coli with α-methylglucoside as substrate","authors":"H. Hagihira, T.H. Wilson, E.C.C. Lin","doi":"10.1016/0006-3002(63)90912-0","DOIUrl":"10.1016/0006-3002(63)90912-0","url":null,"abstract":"<div><p>The properties of the glucose-transport system of <em>Escherichia coli</em> K10 were studied by following intracellular accumulation of <sup>14</sup>C-labeled α-methylglucoside. A mutant defective in the uptake of glucose was found to be unable to accumulate α-methylglucoside to a significant level, confirming the view that the carrier for glucose also acts on α-methylglucoside. Although the glucoside was not incorporated into cellular constituents or metabolized for energy, about one-half of the accumulated molecules underwent phosphorylation while one-half remained as the free glucoside. Studies on the inhibition of uptake of the glucoside showed that the affinity of the compound depended upon the substituents on C-2, C-3 and C-6. Structural modifications at C-1, on the other hand, had relatively little effect on the affinity unless a large aglycone was added. α-Methylglucoside accumulated by the cells was gradually lost upon dilution of the cells in simple inorganic medium. The rate of exit could be accelerated by two groups of compounds: non-metabolizable structural analogs with affinity for the transport carrier and metabolizable compounds which entered the cell by other routes. The effect of the latter group depended upon their further metabolism within the cell rather than their own direct effects on the carrier system.</p></div>","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 3","pages":"Pages 505-515"},"PeriodicalIF":0.0,"publicationDate":"1963-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)90912-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23670749","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 : 1963-11-15DOI: 10.1016/0006-3002(63)90913-2
A.T. Jagendorf , A. Patchornik , M. Sela
Rabbit serum globulins were complexed with bromoacetyl cellulose. Under appropriate conditions 96 to 98% of the protein was chemically bound. Binding of the globulins required a preliminary physical adsorption followed by a chemical reaction. The solid globulin-cellulose complex, under the conditions used, adsorbed specific antigens from solution completely, up to a maximum amount which represented a ratio of antibody to antigen close to that found in a specific precipitate in the equivalence zone. Preliminary experiments are reported on the problems of the specificity of adsorption of homologous antigen compared to unrelated proteins, and of the elution of adsorbed antigen. Potential uses for this method in biochemical investigations are suggested.
{"title":"Use of antibody bound to modified cellulose as an immunospecific adsorbent of antigens","authors":"A.T. Jagendorf , A. Patchornik , M. Sela","doi":"10.1016/0006-3002(63)90913-2","DOIUrl":"10.1016/0006-3002(63)90913-2","url":null,"abstract":"<div><p>Rabbit serum globulins were complexed with bromoacetyl cellulose. Under appropriate conditions 96 to 98% of the protein was chemically bound. Binding of the globulins required a preliminary physical adsorption followed by a chemical reaction. The solid globulin-cellulose complex, under the conditions used, adsorbed specific antigens from solution completely, up to a maximum amount which represented a ratio of antibody to antigen close to that found in a specific precipitate in the equivalence zone. Preliminary experiments are reported on the problems of the specificity of adsorption of homologous antigen compared to unrelated proteins, and of the elution of adsorbed antigen. Potential uses for this method in biochemical investigations are suggested.</p></div>","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 3","pages":"Pages 516-527"},"PeriodicalIF":0.0,"publicationDate":"1963-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)90913-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23670750","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 : 1963-11-15DOI: 10.1016/0006-3002(63)90915-6
Clara Fronticelli, Enrico Bucci
{"title":"Acetone extraction of heme from myoglobin and hemoglobin at acid pH","authors":"Clara Fronticelli, Enrico Bucci","doi":"10.1016/0006-3002(63)90915-6","DOIUrl":"10.1016/0006-3002(63)90915-6","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 3","pages":"Pages 530-531"},"PeriodicalIF":0.0,"publicationDate":"1963-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)90915-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23670752","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}