Zeitschrift fur klinische Chemie und klinische Biochemie最新文献

{"title":"[Determination of iron with CentrifiChem System].","authors":"H G Eisenwiener","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The determination of iron was adapted to the CentrifiChem System. The iron bound to transferrin is freed with a detergent, reduced to Fe++ with sodium dithionite, and determined with bathophenanthroline disulphonate. The operation consists of one run for the blank value and one analytical run. Although the actual reaction time is extremely short, a reaction time of 8--10 min is recommended for both the blank value and the analysis. This ensures adequate clearing during centrifugation under the influence of Teepol. 2 times 100 mul serum are required, and 80 determinations per hour are possible.</p>","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12299816","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 tryptophan metabolism in untreated phenylketonuric patients].","authors":"W Kochen,&nbsp;D J Byrd,&nbsp;R Bühner,&nbsp;E Bühlen","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The products of the oxidative degradation of tryptophan via the kynurenine pathway were quantitatively determined in the urine of ten untreated patients with phenylketonuria, aged 4--35 years. All the patients were sevrely mentally retarded. The results of the analysis suggest a division of the patients into two groups, A and B. The patients of group A showed a basal urinary excretion of kynurenine, kynurenic acid, 3-hydroxykynurenine and xanthurenic acid which lies in the lower part of the normal range. The increase in excretion of tryptophan metabolites under tryptophan loading was, however, significantly less than in controls. On the average, only 0.63 % of the load was excreted in the form of these assayed metabolites; in contrast, the control value is 1,13 %. In group B, the rate of excretion was higher than normal under basal and loading conditions. The post-tryptophan excretion was four times greater than that of controls (4.64 %). 3-hydroxyanthranilic acid could only be detected in group B after loading. The metabolite 8-hydroxyquinaldic acid, which is supposed to be an abnormal metabolic product of tryptophan, was excreted in milligram amounts. The analysis of the metabolites of 3-hydroxyanthranilic acid showed that the excretion of N1-methylnicotinamide and N1-methyl-2-pyridone-5-carboxamide was within the normal range. The excretion of nicotinic acid and its amide was sporadic in both the patients and controls. Other theoretically possible metabolites in the pathway could not be found. A number of unidentified metabolites could be detected by thin-layer chromatography in the basal state. The excretion of these metabolites was greatly augmented after tryptophan loading. Other substances which were not detectable in the basal state became evident on loading. A number of these metabolites are characteristic either of group A or B. The structural identification of one of the new products has been hindered by its instability. A stable cleavage product was identified as omicron-aminoacetophenon by mass-spectroscopy. This metabolite its typical for group B. The possible influence of the blood phenylalanine on the metabolism of tryptophan in phenylketonuria is discussed.</p>","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11343132","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":"[An enzymatic method for the isolation of tubules and cells from human kidney cortex].","authors":"H Bojar,&nbsp;K Balzer,&nbsp;F Boeminghaus,&nbsp;W Staib","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The isolation of tubules and cells from human kidney cortex was realized by an enzymatic method. Tubules and cells were released from slices of kidney cortex by collagenase. The yield amounted to 80 % of the wet weight of incubated cortex slices. Thus numerous experiments with isolated tubules from one organ could be performed. Glucose production from different substrates was measured in order to test the biochemical integrity of the isolated cells. The highest rates of glucose formation were obtained with fructose as precursor. Glucose production was higher from lactate than from pyruvate. With proline and glutamine as substrates only small amounts of glucose were produced. Glucose formation from 10 mmol/1 pyruvate was linear with time up to 80 minutes. Ado-3':5'-P stimulated glucose formation at 10 mumolar concentration and inhibited gluconeogenesis at 1 mmolar, 0.1 mmolar and 1 mumolar concentrations.</p>","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11383166","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":"[Isolation of intact liver parenchymal cells by a modified enzymatic method].","authors":"H Bojar,&nbsp;K Balzer,&nbsp;K Reiners,&nbsp;M Basler,&nbsp;W Reipen,&nbsp;W Staib","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>An enzymatic method is described for isolating intact parenchymal cells from rat livers. 3--4 g cells (wet weight) could be isolated from livers of rats weighing 180--230 g. After an in vitro preperfusion of 15 minutes with a Ca-free buffer, collagenase (200 mg/1) and calcium chloride (5.2 mmol/1) were added. Perfusion was continued for another 15 minutes at 37 degrees C. Micromorphological integrity of cell membranes was demonstrated by scanning electron microscopy. With regard to rates of gluconeogenesis and protein synthesis, parenchymal cells isolated according to our method were found to be superior to liver slices and cells isolated by other methods. Ratios of ATP/ADP (5.69) and of lactate/pyruvate (8.64) as parameters of the energetic situation and the redox state resp. were found within the physiological range. Integrity of cell surface receptors was proved by their sensitivity to epinephrine, glucagon and insulin. Glucagon (0.3 mumol/1) and epinephrine (1 mumol/1) and reduced glycogen deposition in hepatocytes of fasted rats by 84.9 % and 95.9 % resp. Both hormones stimulated glycogenolysis in parenchymal cells of fed rats to a similar extent. Urea synthesis was stimulated 29.5 % by glucagon (1 mumol/1), and inhibited 28.0 % by insulin (10 nmol/1). The stimulatory effect of glucagon (1 mumol/1) was abolished by insulin (10 nmol/1).</p>","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11383291","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":"[Calculation of the parameters of the acid-base balance with the aid of a small computer].","authors":"E Knoll,&nbsp;H Wisser,&nbsp;K Dettmer","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The application and modification of a program published by Hardt (1972), Clin. Chem. 18,658--661) for the calculation of the true pCO2, the standard bicarbonate and the base excess are reported. 217 Determinations of a random patient sample were evaluated graphically, with the aid of a nomogram of Siggaard-Andersen, and mathematically with a computer program. There was good agreement between the two evaluation methods.</p>","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11449707","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":"[Conditions affecting renal excretion of silver by humans. Studies on metabolism of trace elements. VIII].","authors":"D P Mertz,&nbsp;G Wilk,&nbsp;R Koschnick","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The renal excretion of silver was investigated in adult experimental persons of both sexes with normal or variously decreased kidney functions. Silver was measured by emission spectrum analysis. With an indifferent urinary flow of 4.71 plus or minus 2.5 (mean value with standard deviation) ml/min, the mean Ag-excretion was 0.653 plus or minus 0.432 ng/min for a standard 1.73 m2 body surface area. An apparent small increase in the Ag-excretion with increased rate of urine flow could not be statistically confirmed. The widely different Ag-excretion between individuals showed no dependence on the state of diuresis, or on kidney haemodynamic factors down to a decreased inulin clearance of less than 40 ml/min, and a decrease of the PAH clearance to values less than 200 ml/min.</p>","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12299815","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 bacterial degradation of steroids in urine].","authors":"V Graef,&nbsp;M Fuchs,&nbsp;E Balke","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11343133","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":"True Arrhenius relationships of human lactate dehydrogenase.","authors":"M J McQueen","doi":"10.1515/cclm.1975.13.1.17","DOIUrl":"https://doi.org/10.1515/cclm.1975.13.1.17","url":null,"abstract":"<p><p>The pyruvate and NADH concentrations and the buffer pH which gave maximal activity with LDH isoenzymes derived from human heart and liver tissue were established for the temperatures 25 degrees C, 30 degrees C, 35 degrees C, 37 degrees C,, 40 degrees C, 45 degrees C, and 50 degrees C. The velocities of the LDH isoenzymes using these maximal assay conditions were used to obtain Arrhenius plots, i.e. log initial velocity against inverse absolute temperature. The Arrhenius plots were linear with both isoenzyme preparations up to 45 degrees C. Between 45 degrees C and 50 degrees C it appeared that this linear relationship no longer held, particularly with the liver tissue. When the activation energies were calculated both isoenzyme preparations exhibited several points of inflexion, in each case occuring at the same temperatures. These inflexions represent a change in the reaction kinetics, possibly a conformational change in the enzyme. The results also indicate that the LDH 1 and 2 isoenzymes are more efficient than LDH 4 and 5.</p>","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/cclm.1975.13.1.17","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11449705","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":"Comparison of the urinary excretion of aspartate aminotransferase, lactic dehydrogenase, alkaline and acid phosphatases and beta-galactosidase during nephrotoxic serum glomerulonephritis and mercuric chloride tubulonephritis in the rat.","authors":"M Sternberg,&nbsp;I Szlamka,&nbsp;M Moisy,&nbsp;P Rebeyrotte,&nbsp;G Lagrue","doi":"10.1515/cclm.1974.12.12.543","DOIUrl":"https://doi.org/10.1515/cclm.1974.12.12.543","url":null,"abstract":"During tubulonephritis, we observed one sharp excretion peak of all 5 enzymes on day 1. During regeneration of tubular epithelium, lysosomal enzymes decreased below normal level. Isoenzyme analysis gave most interesting results for aspartate aminotransferase: on the first days, while total activity was increased in urine and serum, 2 fractions were found in serum and 3 in urine while only one (cytoplasmic) in normal rat serum; the mitochondria! fraction appeared indicative of tissue necrosis; the third fraction only found in urine migrated towards the anode faster than albumin at pH 8.6 and was never detected in serum. Serum lactic dehydrogenase activity was increased and its isoenzyme pattern was reversed on day 1 when isoenzyme 1 characteristic of kidney cortex predominated. Lactic dehydrogenase isoenzymes 1 and 2 predominated in urine. Urinary enzyme activities after tubular necrosis seem to originate mainly in the cortical tubules. During glomerulonephritis we observed increased urinary activities of the 5 enzymes which culminated during the 2 periods of highest proteinuria: 1) the heterologous phase limited to the first days 2) the autologous phase maximum at the second week. A significant diminution was noted in serum, for alkaline phosphatase during the autologous phase. The only isoenzyme of aspartate aminotransf erase detected in urine at the periods of high enzymuria appeared identical to the isoenzyme present in serum. Urinary enzyme activities during glomerulonephritis appear to originate mainly in the plasma or in the glomeruli.","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1974-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/cclm.1974.12.12.543","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15560616","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":"[Quantitative determination of cystine in the urine of patients with cystinuria (author's transl)].","authors":"G Gundlach,&nbsp;G Hoppe-Seyler,&nbsp;H J Backes","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":23822,"journal":{"name":"Zeitschrift fur klinische Chemie und klinische Biochemie","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1974-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15560619","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}