W Estabrook, J Werringloer, P J O'Brien, J A Peterson
{"title":"Proceedings: The effects of adducts and the nature of activated oxygen for cytochrome P-450 catalyzed hydroxylation reactions.","authors":"W Estabrook, J Werringloer, P J O'Brien, J A Peterson","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"13 8","pages":"373-4"},"PeriodicalIF":0.0,"publicationDate":"1975-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12392374","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.1975.13.7.311
W G Guder, A Habicht, J Kleissl, U Schmidt, O H Wieland
16 Patients with acute right-sided cardiac failure associated with a high pressure of the central venous system, exhibited a marked increase in glutamate dehydrogenase activity in serum. This increase was 40-fold higher than in patients with acute viral hepatitis. Histological examination of seven deceased patients revealed central necrosis within the liver lobule. This observation led us to determine glutamate dehydrogenase activity in microdissected peripheral and central portions from the unchanged liver lobule. A 1.7-fold higher glutamate dehydrogenase activity was found in the central part of the liver lobule than in the peripheral portion. The diagnostic significance of the glutamate dehydrogenase activity distribution along the cords of liver cells is discussed in view of liver diseases with central necrosis.
{"title":"The diagnostic significance of liver cell inhomogeneity: serum enzymes in patients with central liver necrosis and the distribution of glutamate dehydrogenase in normal human liver.","authors":"W G Guder, A Habicht, J Kleissl, U Schmidt, O H Wieland","doi":"10.1515/cclm.1975.13.7.311","DOIUrl":"https://doi.org/10.1515/cclm.1975.13.7.311","url":null,"abstract":"<p><p>16 Patients with acute right-sided cardiac failure associated with a high pressure of the central venous system, exhibited a marked increase in glutamate dehydrogenase activity in serum. This increase was 40-fold higher than in patients with acute viral hepatitis. Histological examination of seven deceased patients revealed central necrosis within the liver lobule. This observation led us to determine glutamate dehydrogenase activity in microdissected peripheral and central portions from the unchanged liver lobule. A 1.7-fold higher glutamate dehydrogenase activity was found in the central part of the liver lobule than in the peripheral portion. The diagnostic significance of the glutamate dehydrogenase activity distribution along the cords of liver cells is discussed in view of liver diseases with central necrosis.</p>","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"13 7","pages":"311-8"},"PeriodicalIF":0.0,"publicationDate":"1975-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/cclm.1975.13.7.311","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12365977","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 fluorometric analysis of 5-hydroxy-indoleacetic acid by condensation with o-phthaldialdehyde has been modified by substituting a HCl-H2SO4 mixture at room temperature for hot concentrated HCl. The sensitivity of the method was increased by a factor of 2.7.
{"title":"[A simplified method for the fluorometric determination of 5-hydroxy-indoleacetic acid in the human liquor cerebrospinalis (author's transl)].","authors":"F Geissbühler","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The fluorometric analysis of 5-hydroxy-indoleacetic acid by condensation with o-phthaldialdehyde has been modified by substituting a HCl-H2SO4 mixture at room temperature for hot concentrated HCl. The sensitivity of the method was increased by a factor of 2.7.</p>","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"13 7","pages":"283-4"},"PeriodicalIF":0.0,"publicationDate":"1975-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12365024","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.1975.13.7.291
U Schwartz, J Hammerstein
A combined adsorption-gel filtration technique has been developed for the quantitation of the cortisol-binding capacity of transcortin: Endogenous steroids are removed from plasma by adsorption on uncoated charcoal. Saturation of the "stripped" binding sites of transcortin is accomplished by equilibrating the sample with a definite amount of labeled cortisol of low specific activity (0.1 muCi/mug). Transcortin-bound [4-14C]cortisol is isolated by gel filtration over Sephadex G-50 at 4 degrees C and measured by liquid scintillation counting. The cortisol-binding capacity of transcortin is calculated directly on the basis of the known specific activity of cortisol. The modification described eliminates methodological disadvantages associated with the original gel filtration procedures, i.e. the possible interference of various endogenous steroids with cortisol binding to transcortin, and the necessity of fluorometric or colorimetric determination of protein-bound cortisol. The values of the cortisol-binding capacity of transcortin in plasma obteined by this simplified assay are in close agreement with results reported in the literature (mean +/- S.D.): healthy males 261 +/- 23 mug/l) of transcortin-bound cortisol (n = 13), healthy nonpregnant females 255 +/- 31 mug/l (n = 15), and pregnant females prior to delivery 560 +/- 82 mug/l (n = 12).
{"title":"A combined adsorption-gel filtration technique for the determination of the cortisol-binding capacity of transcortin.","authors":"U Schwartz, J Hammerstein","doi":"10.1515/cclm.1975.13.7.291","DOIUrl":"https://doi.org/10.1515/cclm.1975.13.7.291","url":null,"abstract":"<p><p>A combined adsorption-gel filtration technique has been developed for the quantitation of the cortisol-binding capacity of transcortin: Endogenous steroids are removed from plasma by adsorption on uncoated charcoal. Saturation of the \"stripped\" binding sites of transcortin is accomplished by equilibrating the sample with a definite amount of labeled cortisol of low specific activity (0.1 muCi/mug). Transcortin-bound [4-14C]cortisol is isolated by gel filtration over Sephadex G-50 at 4 degrees C and measured by liquid scintillation counting. The cortisol-binding capacity of transcortin is calculated directly on the basis of the known specific activity of cortisol. The modification described eliminates methodological disadvantages associated with the original gel filtration procedures, i.e. the possible interference of various endogenous steroids with cortisol binding to transcortin, and the necessity of fluorometric or colorimetric determination of protein-bound cortisol. The values of the cortisol-binding capacity of transcortin in plasma obteined by this simplified assay are in close agreement with results reported in the literature (mean +/- S.D.): healthy males 261 +/- 23 mug/l) of transcortin-bound cortisol (n = 13), healthy nonpregnant females 255 +/- 31 mug/l (n = 15), and pregnant females prior to delivery 560 +/- 82 mug/l (n = 12).</p>","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"13 7","pages":"291-7"},"PeriodicalIF":0.0,"publicationDate":"1975-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/cclm.1975.13.7.291","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12365025","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.1975.13.7.319
M Höller, H Breuer
The influence of fluorocarbon FC 43 on the metabolism of oestrogens in the isolated perfused rat liver was investigated. In comparative once-through perfusions with FC 43 emulsion or albumin solution as perfusion medium, the clearance rates of oestrone and its metabolites were determined. In perfusions with FC 43, the clearance of oestrone was lower, and the metabolites formed in the liver were more concentrated in the outflowing medium than in perfusions without fluorocarbon. This can be explained by the high affinity, even of conjugated oestrogens, to FC 43, which is established by equilibrium dialysis and partition coefficient. The results presented here show that the fluorocarbon has a strong influence of its own on the metabolism of steroids in the isolated perfused liver. Therefore, this solvent should be avoided as medium when the metabolism of steroids is studied in perfusion experiments.
{"title":"The effect of fluorocarbon FC 43 on the metabolism of steroids during perfusion of the isolated rat liver.","authors":"M Höller, H Breuer","doi":"10.1515/cclm.1975.13.7.319","DOIUrl":"https://doi.org/10.1515/cclm.1975.13.7.319","url":null,"abstract":"<p><p>The influence of fluorocarbon FC 43 on the metabolism of oestrogens in the isolated perfused rat liver was investigated. In comparative once-through perfusions with FC 43 emulsion or albumin solution as perfusion medium, the clearance rates of oestrone and its metabolites were determined. In perfusions with FC 43, the clearance of oestrone was lower, and the metabolites formed in the liver were more concentrated in the outflowing medium than in perfusions without fluorocarbon. This can be explained by the high affinity, even of conjugated oestrogens, to FC 43, which is established by equilibrium dialysis and partition coefficient. The results presented here show that the fluorocarbon has a strong influence of its own on the metabolism of steroids in the isolated perfused liver. Therefore, this solvent should be avoided as medium when the metabolism of steroids is studied in perfusion experiments.</p>","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"13 7","pages":"319-23"},"PeriodicalIF":0.0,"publicationDate":"1975-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/cclm.1975.13.7.319","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12365978","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.1975.13.7.285
K von Figura, M Lögering, H Kresse
Assays for the determination of serum alpha-N-acetylglucosaminidase (EC 3.2.1.50) activity are described employing p-nitrophenyl-N-acetyl-alpha-D-glucosaminide, phenyl-N-acetyl-alpha-D-glucosaminide, and UDP-N-acetylglucosamine as substrates. A log normal distribution of the serum enzyme activity was found. The determination of serum alpha-N-acetylglucosaminidase activity proved to be a valuable tool for the recognition of homozygous and heterozygous carriers of the Sanfilippo B gene.
测定血清α -n -乙酰氨基葡萄糖酶(EC 3.2.1.50)活性的方法采用对硝基苯基-n -乙酰基- α - d -氨基葡萄糖、苯基-n -乙酰基- α - d -氨基葡萄糖和udp -n -乙酰氨基葡萄糖作为底物。血清酶活性呈对数正态分布。血清α - n -乙酰氨基葡萄糖酶活性的测定被证明是识别Sanfilippo B基因纯合子和杂合子携带者的有价值的工具。
{"title":"Serum alpha-N-acetylglucosaminidase: determination, characterization, and corrective activity in Sanifilippo B fibroblasts.","authors":"K von Figura, M Lögering, H Kresse","doi":"10.1515/cclm.1975.13.7.285","DOIUrl":"https://doi.org/10.1515/cclm.1975.13.7.285","url":null,"abstract":"<p><p>Assays for the determination of serum alpha-N-acetylglucosaminidase (EC 3.2.1.50) activity are described employing p-nitrophenyl-N-acetyl-alpha-D-glucosaminide, phenyl-N-acetyl-alpha-D-glucosaminide, and UDP-N-acetylglucosamine as substrates. A log normal distribution of the serum enzyme activity was found. The determination of serum alpha-N-acetylglucosaminidase activity proved to be a valuable tool for the recognition of homozygous and heterozygous carriers of the Sanfilippo B gene.</p>","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"13 7","pages":"285-9"},"PeriodicalIF":0.0,"publicationDate":"1975-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/cclm.1975.13.7.285","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11458259","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.1975.13.7.261
E Nieschlag, E J Wickings
This review, based on the current literature, considers the practical aspects of steroid radioimmunoassays. The problems associated with the raising of specific antisera and their characterization are discussed. Features of assay design, reliability criteria and practicability of radioimmunoassays for steroids are considered.
{"title":"A review of radioimmunoassay for steroids.","authors":"E Nieschlag, E J Wickings","doi":"10.1515/cclm.1975.13.7.261","DOIUrl":"https://doi.org/10.1515/cclm.1975.13.7.261","url":null,"abstract":"<p><p>This review, based on the current literature, considers the practical aspects of steroid radioimmunoassays. The problems associated with the raising of specific antisera and their characterization are discussed. Features of assay design, reliability criteria and practicability of radioimmunoassays for steroids are considered.</p>","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":"13 7","pages":"261-71"},"PeriodicalIF":0.0,"publicationDate":"1975-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/cclm.1975.13.7.261","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12365022","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":"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.1975.13.7.273
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}