Pub Date : 1975-07-01DOI: 10.1515/cclm.1975.13.7.305
F Bollengier, A Lowenthal, W Henrotin
The kappa-lambda light chain ratios, the presence of free light chains and the double ring formation, with antikappa and antilambda serum, in single radial immunodiffusion were investigated in serum and cerebrospinal fluid of patients with subacute sclerosing panencephalitis. Cerebrospinal fluid samples of several multiple sclerosis cases were considered simultaneously. The results obtained suggest special immunoglobulin synthesis in both diseases.
{"title":"Bound and free light chains in subacute sclerosing panencephalitis and multiple sclerosis serum and cerebrospinal fluid.","authors":"F Bollengier, A Lowenthal, W Henrotin","doi":"10.1515/cclm.1975.13.7.305","DOIUrl":"https://doi.org/10.1515/cclm.1975.13.7.305","url":null,"abstract":"<p><p>The kappa-lambda light chain ratios, the presence of free light chains and the double ring formation, with antikappa and antilambda serum, in single radial immunodiffusion were investigated in serum and cerebrospinal fluid of patients with subacute sclerosing panencephalitis. Cerebrospinal fluid samples of several multiple sclerosis cases were considered simultaneously. The results obtained suggest special immunoglobulin synthesis in both diseases.</p>","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"13 7","pages":"305-10"},"PeriodicalIF":0.0,"publicationDate":"1975-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/cclm.1975.13.7.305","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11998680","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 : 1975-07-01DOI: 10.1515/cclm.1975.13.7.277
R Schlaeger
Alkaline phosphatase (EC 3.1.3.1) activity increases 5-15 fold in the livers of rats, following bile duct ligation. The mechanism of this increase has been the subject of numerous investigations. In HeLa cells the synthesis of a different phosphatase enzyme protein with higher catalytic activity has been postulated. After preparing an antiserum against rat liver phosphatase, we compared the phosphatase protein concentration in normal and cholestatic livers by immunochemical titration. Our results clearly indicate that the elevation of enzyme activity is due to an increased accumulation of enzyme protein.
{"title":"The mechanism of the increase in the activity of liver alkaline phosphatase in experimental cholestasis: measurement of an increased enzyme concentration by immunochemical titration.","authors":"R Schlaeger","doi":"10.1515/cclm.1975.13.7.277","DOIUrl":"https://doi.org/10.1515/cclm.1975.13.7.277","url":null,"abstract":"<p><p>Alkaline phosphatase (EC 3.1.3.1) activity increases 5-15 fold in the livers of rats, following bile duct ligation. The mechanism of this increase has been the subject of numerous investigations. In HeLa cells the synthesis of a different phosphatase enzyme protein with higher catalytic activity has been postulated. After preparing an antiserum against rat liver phosphatase, we compared the phosphatase protein concentration in normal and cholestatic livers by immunochemical titration. Our results clearly indicate that the elevation of enzyme activity is due to an increased accumulation of enzyme protein.</p>","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"13 7","pages":"277-81"},"PeriodicalIF":0.0,"publicationDate":"1975-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/cclm.1975.13.7.277","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12365023","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 : 1975-07-01DOI: 10.1515/cclm.1975.13.7.299
E Schermuly, M Doss
An improved, specific and sensitive method for the determination of the coproporphyrin isomers I and III is described. In this method, the hydrolysis of the coproporphyrin methyl esters takes place in the silica gel layer of acid-resistant pre-coated thin layer plates. After chromatography in the solvent system 2,6-dimethylpyridine/water, (volume ratio 20 ml + 6 ml), in an ammonia atmosphere, the isomers are measured, either directly in the silica gel layer by fluorimetry, or after elution in 1.0 mol/l hydrochloric acid. The technique makes analysis in the nanogram range possible. See article.
本文描述了一种改进的、特异灵敏的测定同比例卟啉异构体I和III的方法。在这种方法中,卟啉甲酯的水解发生在耐酸预涂薄层板的硅胶层中。在溶剂体系2,6-二甲基吡啶/水(体积比为20 ml + 6 ml)中进行层析后,在氨气氛中直接在硅胶层中用荧光法测量异构体,或在1.0 mol/l盐酸中洗脱后测量异构体。该技术使纳克范围内的分析成为可能。请看文章。
{"title":"Separation of the coprophorphyrin isomers I and III by thin-layer chromatography.","authors":"E Schermuly, M Doss","doi":"10.1515/cclm.1975.13.7.299","DOIUrl":"https://doi.org/10.1515/cclm.1975.13.7.299","url":null,"abstract":"<p><p>An improved, specific and sensitive method for the determination of the coproporphyrin isomers I and III is described. In this method, the hydrolysis of the coproporphyrin methyl esters takes place in the silica gel layer of acid-resistant pre-coated thin layer plates. After chromatography in the solvent system 2,6-dimethylpyridine/water, (volume ratio 20 ml + 6 ml), in an ammonia atmosphere, the isomers are measured, either directly in the silica gel layer by fluorimetry, or after elution in 1.0 mol/l hydrochloric acid. The technique makes analysis in the nanogram range possible. See article.</p>","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"13 7","pages":"299-304"},"PeriodicalIF":0.0,"publicationDate":"1975-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/cclm.1975.13.7.299","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12365976","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}
Eleven parameters in heparinzed whole blood and plasma samples were investigated for storage-dependent changes. Samples were stored at +25 degrees C, and analyses were performed with the SMA 12/60 at 0, 24, 48, 72 and 96 hours after sampling. In whole blood, the following parameters increased significantly during storage: potassium calcium, phosphate, total protein. The following decreased: chloride, CO2, uric acid and bilirubin. In plasma samples, analogous effects were observed for: calcium, CO2, total protein, uric acid and bilirubin.
{"title":"[Errors, resulting from storage, in the determination of 11 parameters in heparinized whole blood and plasma (author's transl)].","authors":"H Keller","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Eleven parameters in heparinzed whole blood and plasma samples were investigated for storage-dependent changes. Samples were stored at +25 degrees C, and analyses were performed with the SMA 12/60 at 0, 24, 48, 72 and 96 hours after sampling. In whole blood, the following parameters increased significantly during storage: potassium calcium, phosphate, total protein. The following decreased: chloride, CO2, uric acid and bilirubin. In plasma samples, analogous effects were observed for: calcium, CO2, total protein, uric acid and bilirubin.</p>","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"13 6","pages":"217-24"},"PeriodicalIF":0.0,"publicationDate":"1975-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12387732","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 : 1975-06-01DOI: 10.1515/cclm.1975.13.6.225
D Seiler, W Fiehn, E Kuhn
Desmosterol is found in various organs of rats that show signs of myotonia in their skeletal muscle as a result of treatment with 20.25-diazacholesterol. The amount of desmosterol depends on the time of treatment, and is different in different organs and different kinds of muscle. The increase in desmosterol is much lower and the rats do not show any signs of myotonia when fed a cholesterol rich diet in addition to treatment with 20.25-diazacholesterol. Treatment with triparanol also causes desmosterol accumulation but in these rats myotonia is rarely observed. Our results suggest that in the experimental animals myotonia becomes manifest when every second cholesterol molecule of the muscle cell membrane is replaced by desmosterol. This is easily achieved in animals fed with 20.25-diazacholesterol but rarely occurs with triparanol.
{"title":"Desmosterol accumulation in rats with experimental myotonia.","authors":"D Seiler, W Fiehn, E Kuhn","doi":"10.1515/cclm.1975.13.6.225","DOIUrl":"https://doi.org/10.1515/cclm.1975.13.6.225","url":null,"abstract":"Desmosterol is found in various organs of rats that show signs of myotonia in their skeletal muscle as a result of treatment with 20.25-diazacholesterol. The amount of desmosterol depends on the time of treatment, and is different in different organs and different kinds of muscle. The increase in desmosterol is much lower and the rats do not show any signs of myotonia when fed a cholesterol rich diet in addition to treatment with 20.25-diazacholesterol. Treatment with triparanol also causes desmosterol accumulation but in these rats myotonia is rarely observed. Our results suggest that in the experimental animals myotonia becomes manifest when every second cholesterol molecule of the muscle cell membrane is replaced by desmosterol. This is easily achieved in animals fed with 20.25-diazacholesterol but rarely occurs with triparanol.","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"13 6","pages":"225-9"},"PeriodicalIF":0.0,"publicationDate":"1975-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/cclm.1975.13.6.225","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12387733","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 hitherto unknown substance, which appears between glycine and alanine in ion exchange chromatograms, was found in the erythrocyte cold haemolysate of two children with metachromatic leucodystophy; this substance could not be detected in the haemolysates from patients with other (brain) diseases. It would be worthwhile to test for this symptom in confirmed, still active (florid) cases of metachromatic leucodystrophy.
{"title":"[Detection of a hitherto unknown ninhydrin positive substance in the haemolysate of patients with metachromatic leucodystrophy (author's transl)].","authors":"G W Schmidt","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A hitherto unknown substance, which appears between glycine and alanine in ion exchange chromatograms, was found in the erythrocyte cold haemolysate of two children with metachromatic leucodystophy; this substance could not be detected in the haemolysates from patients with other (brain) diseases. It would be worthwhile to test for this symptom in confirmed, still active (florid) cases of metachromatic leucodystrophy.</p>","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"13 6","pages":"239-40"},"PeriodicalIF":0.0,"publicationDate":"1975-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12416579","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":"[Quantitation of lipids in blood, plasma and tissues by gas-liquid chromatography (author's transl)].","authors":"M Radke, H Schäfer, J D Kruse-Jarres","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"13 6","pages":"231-7"},"PeriodicalIF":0.0,"publicationDate":"1975-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12387734","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 relationship between temperature and the behaviour of aspartate aminotransferase was investigated in the presence of pyridoxal 5'-phosphate. The addition in vitro of pyridoxal 5'-phosphate caused an increase in the activity and altered the thermal behaviour of aspartate aminotransferase. In choosing the temperature for the determination of enzymic activity, the concentration of the coenzyme must therefore also be considered.
{"title":"[The influence of pyridoxal 5'-phosphate on the temperature relationships of aspartate aminotransferase isoenzymes].","authors":"K Jung, B Lüdtke, E Egger","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The relationship between temperature and the behaviour of aspartate aminotransferase was investigated in the presence of pyridoxal 5'-phosphate. The addition in vitro of pyridoxal 5'-phosphate caused an increase in the activity and altered the thermal behaviour of aspartate aminotransferase. In choosing the temperature for the determination of enzymic activity, the concentration of the coenzyme must therefore also be considered.</p>","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"13 5","pages":"179-81"},"PeriodicalIF":0.0,"publicationDate":"1975-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12386851","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}
H Küffer, R Richterich, R Kraft, E Peheim, J P Colombo
1. A mercury(II)-thiocyanate method for the determination of chloride in plasma and serum was adapted for the Greiner Electronic Selective Analyzer GSA II. A sample blank value and a partial reagent blank value were determined by omitting thiocyanate from the control system. 2. The course of the reaction was investigated. For a reaction time of 350-500 s, the response was linear between 30 and 130 mmol/l. Between 90 and 110 mmol/l, the deviation between the actual and the theoretical value is less than 1%. 3. The calibration must be checked and, if necessary, restandardized; this is probably due to variable contamination of the reagents with chloride ions. 4. Haemolysis, lipaemia and bilirubin do not interfere. Protein has no effect on the course of the reaction. 5. At concentrations around 100 mmol/l, the in series precision, expressed as the variation coefficient (%), is 0.3-0.6% for aqueous solutions, 0.4-0.8% for liquid control sera, and 0.8-1.5% for lyophilized control sera. 6. No carry over was detectable from samples containing 150 to those containing 10 mmol/l.
{"title":"[The determination of chloride in plasma and serum (mercury(II)-thiocyanate method) with the Greiner Electronic Selective Analyzer GSA II (author's transl)].","authors":"H Küffer, R Richterich, R Kraft, E Peheim, J P Colombo","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>1. A mercury(II)-thiocyanate method for the determination of chloride in plasma and serum was adapted for the Greiner Electronic Selective Analyzer GSA II. A sample blank value and a partial reagent blank value were determined by omitting thiocyanate from the control system. 2. The course of the reaction was investigated. For a reaction time of 350-500 s, the response was linear between 30 and 130 mmol/l. Between 90 and 110 mmol/l, the deviation between the actual and the theoretical value is less than 1%. 3. The calibration must be checked and, if necessary, restandardized; this is probably due to variable contamination of the reagents with chloride ions. 4. Haemolysis, lipaemia and bilirubin do not interfere. Protein has no effect on the course of the reaction. 5. At concentrations around 100 mmol/l, the in series precision, expressed as the variation coefficient (%), is 0.3-0.6% for aqueous solutions, 0.4-0.8% for liquid control sera, and 0.8-1.5% for lyophilized control sera. 6. No carry over was detectable from samples containing 150 to those containing 10 mmol/l.</p>","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"13 5","pages":"203-11"},"PeriodicalIF":0.0,"publicationDate":"1975-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12387730","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}