{"title":"THE PURIFICATION OF BEEF THYROGLOBULIN WITH THE USE OF GEL FILTRATION.","authors":"L PERELMUTTER, W DEVLIN, N R STEPHENSON","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":9531,"journal":{"name":"Canadian journal of biochemistry and physiology","volume":"41 ","pages":"2493-500"},"PeriodicalIF":0.0,"publicationDate":"1963-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23684167","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":"ELECTROPHORESIS OF HISTONES ON POLYACRYLAMIDE GELS.","authors":"A DRIEDGER, L D JOHNSON, A M MARKO","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":9531,"journal":{"name":"Canadian journal of biochemistry and physiology","volume":"41 ","pages":"2507-16"},"PeriodicalIF":0.0,"publicationDate":"1963-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23684169","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}
Metabolically active mitochondria were isolated from pigeon breast muscle in cold 0.45 M sucrose with ATP, EDTA, and tris buffer at pH 7.4. Fresh mitochondria were analyzed for sodium, potassium, nitrogen, iron, and water. They were morphologically intact and showed respiratory control, respiration being limited by the phosphate acceptor and stimulated by dinitrophenol. The respiratory rate was the same in the Warburg respirometer as that in the polarograph chamber; no effect of agitation was observed. The rates of oxygen consumption over short periods of time were 30–40 μ atoms per hour per mg N for α-keto-glutarate and glutamate, 16 for malate, and 1.3 for β-OH butyrate; except in the last case, satisfactory P/O ratios were obtained. A soluble, heat-stable muscle factor, not precipitated at 100,000 × G, stimulated respiration with each substrate but did not affect phosphorylation. From optical density measurements of muscle mitochondria they appeared to behave as moderately good osmometers; only slight ...
{"title":"PIGEON MUSCLE MITOCHONDRIA: ION CONCENTRATIONS, OXIDATIVE PHOSPHORYLATION, SWELLING, AND EXTRAPARTICULATE SPACE.","authors":"G. J. Marcus, J. Manery","doi":"10.1139/O63-283","DOIUrl":"https://doi.org/10.1139/O63-283","url":null,"abstract":"Metabolically active mitochondria were isolated from pigeon breast muscle in cold 0.45 M sucrose with ATP, EDTA, and tris buffer at pH 7.4. Fresh mitochondria were analyzed for sodium, potassium, nitrogen, iron, and water. They were morphologically intact and showed respiratory control, respiration being limited by the phosphate acceptor and stimulated by dinitrophenol. The respiratory rate was the same in the Warburg respirometer as that in the polarograph chamber; no effect of agitation was observed. The rates of oxygen consumption over short periods of time were 30–40 μ atoms per hour per mg N for α-keto-glutarate and glutamate, 16 for malate, and 1.3 for β-OH butyrate; except in the last case, satisfactory P/O ratios were obtained. A soluble, heat-stable muscle factor, not precipitated at 100,000 × G, stimulated respiration with each substrate but did not affect phosphorylation. From optical density measurements of muscle mitochondria they appeared to behave as moderately good osmometers; only slight ...","PeriodicalId":9531,"journal":{"name":"Canadian journal of biochemistry and physiology","volume":"208 1","pages":"2529-42"},"PeriodicalIF":0.0,"publicationDate":"1963-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76752173","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 RELEASE OF ACETYLCHOLINE FROM A SYMPATHETIC GANGLION BY CARBACHOL. RELATIONSHIP TO THE FUNCTIONAL SIGNIFICANCE OF THE LOCALIZATION OF ACETYLCHOLINESTERASE.","authors":"D N MCKINSTRY, E KOENIG, W A KOELLE, G B KOELLE","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":9531,"journal":{"name":"Canadian journal of biochemistry and physiology","volume":"41 ","pages":"2599-609"},"PeriodicalIF":0.0,"publicationDate":"1963-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23683856","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 CYTOLOGICAL LOCALIZATION OF HUMAN CHORIONIC GONADOTROPIN.","authors":"A LEZNOFF, B A DAVIS","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":9531,"journal":{"name":"Canadian journal of biochemistry and physiology","volume":"41 ","pages":"2517-21"},"PeriodicalIF":0.0,"publicationDate":"1963-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23684170","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 activity of serum ribonuclease (RNase) of rats fed a diet containing 4-dimethylaminoazobenzene was depressed by 50–60% at the third week of feeding compared to that of control rats fed the basal diet alone for the same period of time. Tumor cells of the Novikoff hepatoma contained 7–8% of the RXase activity of normal liver cells.
{"title":"SERUM RIBONUCLEASE DURING THE PROCESS OF DAB CARCINOGENESIS AND TUMOR GROWTH.","authors":"J. Zytko, A. Cantero","doi":"10.1139/O63-269","DOIUrl":"https://doi.org/10.1139/O63-269","url":null,"abstract":"The activity of serum ribonuclease (RNase) of rats fed a diet containing 4-dimethylaminoazobenzene was depressed by 50–60% at the third week of feeding compared to that of control rats fed the basal diet alone for the same period of time. Tumor cells of the Novikoff hepatoma contained 7–8% of the RXase activity of normal liver cells.","PeriodicalId":9531,"journal":{"name":"Canadian journal of biochemistry and physiology","volume":"83 7 1","pages":"2391-6"},"PeriodicalIF":0.0,"publicationDate":"1963-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87654563","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}
Blood sugar changes in fish, after the intravenous injection of alloxan, were determined by a modified Folin method and by an enzymatic method using glucose oxidase. The rest reduction was calculated as the difference between the two methods. The blood rest reduction levels were normally 15 mg% in toadfish and 11 mg% in bullheads (glucose 19 and 22 mg% respectively). One hour after alloxan administration, the rest reduction had increased on the average several times while the glucose level was only slightly above normal. From a maximum at 1 hour the rest reduction level dropped while the glucose level began to rise. Considerable variation in the response to alloxan occurred.The reducing substances in the blood were studied by paper chromatography. In normal blood, glucose and another compound (Rf value approximately one-half that of glucose) were detected by alkaline silver nitrate. No increase in reducing material in alloxan-treated samples could be shown on the chromato-grams by the methods used.
{"title":"REDUCING SUBSTANCES IN THE BLOOD OF NORMAL AND ALLOXAN-TREATED FISH.","authors":"M. Moule, P. F. Nace","doi":"10.1139/Y63-270","DOIUrl":"https://doi.org/10.1139/Y63-270","url":null,"abstract":"Blood sugar changes in fish, after the intravenous injection of alloxan, were determined by a modified Folin method and by an enzymatic method using glucose oxidase. The rest reduction was calculated as the difference between the two methods. The blood rest reduction levels were normally 15 mg% in toadfish and 11 mg% in bullheads (glucose 19 and 22 mg% respectively). One hour after alloxan administration, the rest reduction had increased on the average several times while the glucose level was only slightly above normal. From a maximum at 1 hour the rest reduction level dropped while the glucose level began to rise. Considerable variation in the response to alloxan occurred.The reducing substances in the blood were studied by paper chromatography. In normal blood, glucose and another compound (Rf value approximately one-half that of glucose) were detected by alkaline silver nitrate. No increase in reducing material in alloxan-treated samples could be shown on the chromato-grams by the methods used.","PeriodicalId":9531,"journal":{"name":"Canadian journal of biochemistry and physiology","volume":"19 1","pages":"2397-407"},"PeriodicalIF":0.0,"publicationDate":"1963-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89727710","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}
Evidence is presented refuting the possibility that pyruvylcholine might be a transmitter in cholinergic transmission processes.The physiology and pharmacology of acetylcholine release is discussed, with special reference to recent work.Experiments on the output of acetylcholine from electrically stimulated ileum preparations are described. It is suggested that two output mechanisms may exist: one important at low firing rates, which yields a constant output of transmitter per unit time and is morphine-sensitive; the other brought in at higher frequencies of excitation, which yields a more nearly constant volley output, and is morphine-resistant.
{"title":"CHOLINERGIC TRANSMISSION AND ACETYLCHOLINE OUTPUT.","authors":"W. D. Paton","doi":"10.1139/O63-294","DOIUrl":"https://doi.org/10.1139/O63-294","url":null,"abstract":"Evidence is presented refuting the possibility that pyruvylcholine might be a transmitter in cholinergic transmission processes.The physiology and pharmacology of acetylcholine release is discussed, with special reference to recent work.Experiments on the output of acetylcholine from electrically stimulated ileum preparations are described. It is suggested that two output mechanisms may exist: one important at low firing rates, which yields a constant output of transmitter per unit time and is morphine-sensitive; the other brought in at higher frequencies of excitation, which yields a more nearly constant volley output, and is morphine-resistant.","PeriodicalId":9531,"journal":{"name":"Canadian journal of biochemistry and physiology","volume":"35 1","pages":"2637-53"},"PeriodicalIF":0.0,"publicationDate":"1963-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"85770640","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":"ACETYLCHOLINE IN INVERTEBRATE NERVOUS SYSTEMS.","authors":"E FLOREY","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":9531,"journal":{"name":"Canadian journal of biochemistry and physiology","volume":"41 ","pages":"2619-26"},"PeriodicalIF":0.0,"publicationDate":"1963-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23683857","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}
A procedure is described for retaining bovine plasma Ac-globulin activity as one part of the protein from plasma for every 1000 parts removed. The yields averaged 15%. The procedure involves removal of prothrombin with barium carbonate, isoelectric fractionation, fractionation with ammonium sulphate, chromatography on Amberlite IRC-50, and a second fractionation with ammonium sulphate. The procedure requires 2 days; however, the first day completes up to chromatography and the concentrate at that time is quite useful for many purposes. It is more stable than the product obtained after chromatography and the yields are higher. In absence of salts Ac-globulin is quite insoluble at pH 5.0. The final product usually contained some impurity. With the analytical ultra-centrifuge the S20 in 0.1 M potassium chloride solution was found to be 4.2 at a protein concentration of 12.4 mg/ml. The specific activity was 1500 U./mg dry weight. Bovine plasma contains 120 U./ml or about 9 mg/100 ml. Assuming the same specifi...
{"title":"PROPERTIES OF BOVINE AC-GLOBULIN CONCENTRATES AND METHODS OF PREPARATION.","authors":"N. Aoki, C. Harmison, W. Seegers","doi":"10.1139/O63-271","DOIUrl":"https://doi.org/10.1139/O63-271","url":null,"abstract":"A procedure is described for retaining bovine plasma Ac-globulin activity as one part of the protein from plasma for every 1000 parts removed. The yields averaged 15%. The procedure involves removal of prothrombin with barium carbonate, isoelectric fractionation, fractionation with ammonium sulphate, chromatography on Amberlite IRC-50, and a second fractionation with ammonium sulphate. The procedure requires 2 days; however, the first day completes up to chromatography and the concentrate at that time is quite useful for many purposes. It is more stable than the product obtained after chromatography and the yields are higher. In absence of salts Ac-globulin is quite insoluble at pH 5.0. The final product usually contained some impurity. With the analytical ultra-centrifuge the S20 in 0.1 M potassium chloride solution was found to be 4.2 at a protein concentration of 12.4 mg/ml. The specific activity was 1500 U./mg dry weight. Bovine plasma contains 120 U./ml or about 9 mg/100 ml. Assuming the same specifi...","PeriodicalId":9531,"journal":{"name":"Canadian journal of biochemistry and physiology","volume":"66 1","pages":"2409-21"},"PeriodicalIF":0.0,"publicationDate":"1963-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75077518","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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