Biomedical subjects
Publications and source records attributed to H Rosenmund.
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Myoglobin and the enzymatic activity of creatine phosphokinase CK), MB-isoenzyme of CK (CK-MB), aspartate aminotransferase (GOT), alanine aminotransferase (GPT) and lactic acid dehydrogenase (LDH) were serially determined in 10 patients with acute myocardial infarction. Additionally the same parameters were assessed in 5 patients with angina pectoris for 24 hours after bicycle ergometry. 10 in-patients served as controls. Myoglobin was determined by radioimmunoassay and the other enzyme activities according to the current kinetic methods. Comparison of myoglobin with the enzymatic parameters showed that the myoglobin peak occurs 5.6 hours after the beginning of the sampling period, i.e. 7.3 hours earlier than CK and CK-MB and 11.6 hours earlier than GOT. In analogy to this finding the descending limb of the myoglobin curve was significantly earlier at a level of one third of the peak value, i.e. 8.2 hours earlier than CK-MB, 18.8 hours earlier than CK and 27.3 hours earlier than GOT. No signs of myocardial necrosis in terms of myoglobin or enzymatic activity could be detected after bicycle ergometry. It is concluded that myoglobin is a more sensitive parameter for assessment of the acute phase in patients with myocardial infarction than the usualy enzymatic parameters.
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The inhibition test shows elevated creatine kinase MB (CK-MB) activity if the test volume is reduced. Hence, sera with considerably increased serum protein values may produce negative CK-MB results. What is involved here is an apparent blank phenomenon dependent on the serum proteins. This effect is not derived from the Inh-CK-M antibody but is directly connected with the CK-reagents, since analogous relationships are also shown with the conventional CK-method. In order to produce reliable inhibition test results, a reflectant blank versus test-volume and serum protein level must be taken into account.
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The hydrolytic properties of the isoenzymes of human pancreatic and salivary alpha-amylase (1,4-glucan 4-glucanohydrolase, EC 3.2.1.1) were studied. The eight pancreatic isoenzymes split glycogen and starch into glucose, maltose, maltotriose, maltotetraose and oligosaccharides of 5-10 glucose units. Maltotetraose is further digested to lower homologues. The percentage of conversion to those products is dependent on the substrate and varies from one isoenzyme to another. The six salivary isoenzymes split glycogen and starch into maltose, maltotriose, maltotetraose, pannose and oligosaccharides of 5--10 glucose units. Maltotetraose and pannose are further digested to lower homologues. The percentage of conversion to these products is dependent on the substrate and is specific for each isoenzyme.
A macroamylase complex has been artificially generated by combining purified pancreatic and salivary alpha-amylase solutions with physiological amounts of human gamma-globulin. This complex was only partially dissociable at pH 3.5. Salivary alpha-amylase was shown to have higher binding affinity to gamma-globulin than the pancreatic alpha-amylase. Small amounts of macroamylase complex were also formed after the addition of purified salivary or pancreatic alpha-amylase to normal serum. This effect was more distinct when salivary alpha-amylase was added. Electrophoretic examination of serum proteins from subjects with macroamylasemia showed a significant increase of gamma-globulin fraction. Seromucoid of these subjects was also above normal range. Electrophoresis of serum glycoproteins yielded raised values of the fraction moving with gamma-globulin.
A semiautomated fluorometric method for the quantitative determination of urinary dopa, 3-(3,4-dihydroxyphenyl)-L-alanine, is described. It provides a simple, sensitive and reproducible analytical technique for routine use. Dopa is isolated from interfering substances, especially catecholamines, by adsorption onto aluminium oxide, elution with 0.1 M HCl, then passed through a cation-exchange column. By mild oxidation with potassium ferricyanide, dopa is cyclized to dopachrome. This is isomerised with strong alkali to 5,6-substituted indole, which is highly fluorescent but very unstable in the presence of oxygen. The addition of ascorbic acid and 3-mercaptopropionic acid to the alkaline solution stabilizes the fluorescence. Concentrations of chemicals, pH and reaction times are made optimal for maximal sensitivity. Recovery of dopa added to the urine samples averaged 79% (range, 75 to 83). Reproducibility of results from the same urine specimen gave a coefficient of variation of 2.4%. In healthy adults, we found daily excretion ranges from 17.3 to 54.9 (mean: 36.1) microng/24 h or from 0.015 to 0.048 (mean: 0.021) microng/mg cretinine.
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Human salivary and pancreatic alpha-amylase (1,4-glucan 4-glucanohydrolase, EC 3.2.1.1) were separated by electrofocusing. In the first case we obtained six isoenzymes with isoelectric points of pH 5.70, 5.72, 6.23, 6.32, 6.73 and 6.88. Human pancreatic alpha-amylase has been separated into eight isoenzymes with isoelectric points of pH 5.72, 5.77, 5.88, 6.05, 6.23, 6.69, 6.72 and 6.95. Some of the isoenzymes were shown to be sialoproteins; others representing about 80% of the total activity did not contain neuraminic acid. The molecular weight of the non-sialoproteinic isoenzymes was found to be about 47 000 in all cases.
The enzymic determination of total cholesterol described by P. Röschlau (Z. Klin. Chem. Klin. Biochem. 12, 403-407 (1974)) was modified and adapted to the Centrifichem system. The method which requires only 5 mul serum, is accurate, quick and simple. A separate serum blank is not necessary. Compared with the manual method, smaller quantities of reagents used and the resulting decrease in cost are appreciable for large series of analyses. The course of the reaction at 30 and 37 degrees C, the linearity, calibration, precision, recovery, and correlation with the Lieberman-Burchard method and the enzymic manual method are described.
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