{"title":"A simple method for clearing lipemic sera by lipid extraction.","authors":"G Hillmann","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"13 7","pages":"327-8"},"PeriodicalIF":0.0,"publicationDate":"1975-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11389912","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.1975.13.7.305
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.1975.13.7.273
E S Markianos, I E Nyström
A method for the estimation of dopamine beta-hydroxylase activity in human serum is described, based on a thin layer chromatographic separation of the substrate ([14C]tyramine) from the reaction product ([14C]octopamine). The basic properties of the human serum enzyme, investigated by this method are described.
{"title":"Serum dopamine beta-hydroxylase: assay and enzyme properties.","authors":"E S Markianos, I E Nyström","doi":"10.1515/cclm.1975.13.7.273","DOIUrl":"https://doi.org/10.1515/cclm.1975.13.7.273","url":null,"abstract":"<p><p>A method for the estimation of dopamine beta-hydroxylase activity in human serum is described, based on a thin layer chromatographic separation of the substrate ([14C]tyramine) from the reaction product ([14C]octopamine). The basic properties of the human serum enzyme, investigated by this method are described.</p>","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"13 7","pages":"273-6"},"PeriodicalIF":0.0,"publicationDate":"1975-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/cclm.1975.13.7.273","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11458258","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}