Homogenates of rat and frog liver were incubated with ThDP and ThMP at different pHs. The products of hydrolysis were identified by paper chromatography. In experiments carried out at pH 9 with ThDP as substrate in the presence of rat liver, the spot corresponding to Th did not appear on the chromatogram. This was in contrast with parallel experiments with frog liver. ThMP from commercial source behaved differently toward enzymatic decomposition than ThMP originating from hydrolysis of ThDP. Attempts have been made to explain these differences.
{"title":"The influence of rat and frog liver enzymes on the hydrolysis of ortho and pyrophosphoric esters of thiamine","authors":"Rina Singer-Altbeker, A. Ber","doi":"10.1002/JCP.1030660111","DOIUrl":"https://doi.org/10.1002/JCP.1030660111","url":null,"abstract":"Homogenates of rat and frog liver were incubated with ThDP and ThMP at different pHs. \u0000 \u0000The products of hydrolysis were identified by paper chromatography. \u0000 \u0000In experiments carried out at pH 9 with ThDP as substrate in the presence of rat liver, the spot corresponding to Th did not appear on the chromatogram. This was in contrast with parallel experiments with frog liver. ThMP from commercial source behaved differently toward enzymatic decomposition than ThMP originating from hydrolysis of ThDP. Attempts have been made to explain these differences.","PeriodicalId":50243,"journal":{"name":"Journal of Cellular and Comparative Physiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1965-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/JCP.1030660111","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"50891219","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}
The glycolytic enzymes, lactic dehydrogenase and aldolase, usually thought to be freely dissolved in the sarcoplasmic matrix, are in good part attached to the muscle ultrastructure. This attachment becomes manifest when the enzyme activities and specific activities of the press juices of whole skeletal muscles (rabbit) are compared with those of minced muscles, all obtained by ultracentrifugation of the tissues at 40,000 xpm for 16 to 20 hours. Mincing causes a great increase in the activities, associated with a rise in the volume and protein concentration of the press juices. We interpret these increases to be due to the solution in the matrix of enzymes previously attached to the ultrastructure. The same conclusion is reached by a different method, which we call “washing the ultrastructure.” It consists in multiple centrifugations of whole skeletal muscles, and removal of press juices, alternating with periods of imbibition of a buffer (0.1 M phosphate at pH 7.5) too dilute to dissolve out the fibrous proteins. During the imbibitions enzymes diffuse out into the buffer not imbibed, which becomes an extract. After four centrifugation-imbibition sequences in as many days nearly all of the fluid matrix has been replaced by buffer. Enzyme activities fall steeply in press juices and extracts until nearly all freely dissolved enzymes have been washed away. Homogenates of the pressed muscles then show activities which are about half of those found in the homogenates of unpressed control muscles. We conclude that the enzymes found in the homogenates of the pressed muscles have previously been attached to the ultrastructure. Similar experiments with heart muscle indicate that nearly all of these enzymes are normally attached to the ultrastructure. Press juices contain only traces of activity, even after the heart has been minced. A fraction of the enzymes is slowly detached during the centrifugation-imbibition sequences, appearing mainly in the extracts.
{"title":"The attachment of glycolytic enzymes to muscle ultrastructure","authors":"W. R. Amberson, F. Roisen, A. C. Bauer","doi":"10.1002/JCP.1030660108","DOIUrl":"https://doi.org/10.1002/JCP.1030660108","url":null,"abstract":"The glycolytic enzymes, lactic dehydrogenase and aldolase, usually thought to be freely dissolved in the sarcoplasmic matrix, are in good part attached to the muscle ultrastructure. This attachment becomes manifest when the enzyme activities and specific activities of the press juices of whole skeletal muscles (rabbit) are compared with those of minced muscles, all obtained by ultracentrifugation of the tissues at 40,000 xpm for 16 to 20 hours. Mincing causes a great increase in the activities, associated with a rise in the volume and protein concentration of the press juices. We interpret these increases to be due to the solution in the matrix of enzymes previously attached to the ultrastructure. \u0000 \u0000 \u0000 \u0000The same conclusion is reached by a different method, which we call “washing the ultrastructure.” It consists in multiple centrifugations of whole skeletal muscles, and removal of press juices, alternating with periods of imbibition of a buffer (0.1 M phosphate at pH 7.5) too dilute to dissolve out the fibrous proteins. During the imbibitions enzymes diffuse out into the buffer not imbibed, which becomes an extract. After four centrifugation-imbibition sequences in as many days nearly all of the fluid matrix has been replaced by buffer. Enzyme activities fall steeply in press juices and extracts until nearly all freely dissolved enzymes have been washed away. Homogenates of the pressed muscles then show activities which are about half of those found in the homogenates of unpressed control muscles. We conclude that the enzymes found in the homogenates of the pressed muscles have previously been attached to the ultrastructure. \u0000 \u0000 \u0000 \u0000Similar experiments with heart muscle indicate that nearly all of these enzymes are normally attached to the ultrastructure. Press juices contain only traces of activity, even after the heart has been minced. A fraction of the enzymes is slowly detached during the centrifugation-imbibition sequences, appearing mainly in the extracts.","PeriodicalId":50243,"journal":{"name":"Journal of Cellular and Comparative Physiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1965-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/JCP.1030660108","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"50891671","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":"PHYSICAL CHANGES AND MUTAGENESIS.","authors":"R B Setlow","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":50243,"journal":{"name":"Journal of Cellular and Comparative Physiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1964-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23771529","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 PATTERNS OF NUCLEIC ACID AND PROTEIN SYNTHESIS CAUSED BY A PURINE ANALOGUE.","authors":"H Chantrenne","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":50243,"journal":{"name":"Journal of Cellular and Comparative Physiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1964-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23769952","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":"REACTION OF SOME MUTAGENIC AND CARCINOGENIC COMPOUNDS WITH NUCLEIC ACIDS.","authors":"P Brookes, P D Lawley","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":50243,"journal":{"name":"Journal of Cellular and Comparative Physiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1964-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23769950","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":"ORIGIN AND NATURE OF SPONTANEOUS MUTATIONS IN MEIOTIC ORGANISMS.","authors":"G E Magni","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":50243,"journal":{"name":"Journal of Cellular and Comparative Physiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1964-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23769953","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":"ACRIDINE MUTAGENS AND DNA STRUCTURE.","authors":"L S Lerman","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":50243,"journal":{"name":"Journal of Cellular and Comparative Physiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1964-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23771525","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 MOLECULAR MECHANISM OF HYDROCARBON CARCINOGENESIS.","authors":"C Heidelberger","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":50243,"journal":{"name":"Journal of Cellular and Comparative Physiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1964-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23769951","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 INDUCTION OF MUTATIONS IN BACTERIOPHAGE T4 BY ULTRAVIOLET IRRADIATION AND BY PROFLAVIN.","authors":"J W Drake","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":50243,"journal":{"name":"Journal of Cellular and Comparative Physiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1964-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23771524","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":"SYMPOSIUM ON MOLECULAR ACTION OF MUTAGENIC AND CARCINOGENIC AGENTS.","authors":"L S Lerman","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":50243,"journal":{"name":"Journal of Cellular and Comparative Physiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1964-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23771526","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}
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