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Biomedical subjects

A Jung

Publications and source records attributed to A Jung.

At least 199 records · Page 11Linked to original sources
PubMed1975

[Significance and margin of error of echoventriculography in children up to 3 years of age].

Comparative ventricular measurements were made on 43 small children and infants between the ages of 0 and 3 years, the methods used being those of pneumoencephalography and enchoventriculography. The number of cases that could be analyzed was 31. Good agreement of the results for the third ventricle was obtained in 64.5 per cent and for the lateral ventricular index, in 80.6 per cent of the cases. More or less satisfactory agreement of the two methods provides against making a clear decision in favor of one or the other method. Good agreement was observed between the results of repeated echoventriculographic examinations on 31 normal children. From these results as well as from th results of echographic examination on hydrocephalic children it can be concluded that echoventriculography is a reliable method of diagnosis even in those cases in which it is routinely applied to both inpatients and outpatients.

Child, Preschool↗
PubMed1975

[DNA-, RNA-, lipidsynthesis and the specific activity of the glucose-6-phosphate dehydrogenase and glucose-6-phosphatase in the different morphologic stages of Plasmodium vinckei].

DNA-, RNA-, and lipidsynthesis, glucose-6-phosphate-dehydrogenase, glucose-6-phosphatase and succinate-dehydrogenase were studied in the different morphologic stages of blood schizogony of Plasmodium vinckei. For the separation of these stages of the maturation cycle a discontinuous Ficoll-density gradient was developed. By this method the morphologic stages were separated and obtained in sufficient amounts. DNA-, RNA- and lipidsynthesis was not continuous in the intraerythrocytic cycle of the parasite. The glucose-6-phosphate dehydrogenase activity of the infected erythrocytes decreases whereas that of the glucose-6-phosphatase increases in the maturation cycle of P. vinckei.

Animals↗
PubMed1975

[15-Hydroxyprostaglandin dehydrogenase from human placenta, II. Steady state kinetics and influence of prostaglandin F2alpha analogues (author's transl)].

A complete initial rate analysis of the forward reaction catalyzed by 15-hydroxyprostaglandin dehydrogenase from human term placenta was carried out at pH 7.4 (100mM triethanolamine) with the substrates NAD, and the prostaglandins E1, E2 and F2alpha. The limiting Michaelis constants, the dissociation constants, and the limiting maximum velocities for these substrates were calculated by fitting the obtained data by weighted linear regression analysis to the complete rate equation. The product inhibition of the reaction by NADH and 15-oxoprostaglandin was studied and the inhibition constants were graphically determined. The initial rate and inhibition patterns obtained indicate that the reaction follows kinetically an ordered Bi Bi mechanism. The prostaglandin F2alpha analogues ICI 81,008 and ICI 79,939 were not utilized by the enzyme. With ICI 81,008 a slight inhibition of the enzymatic reaction with prostaglandin F2alpha was observed, whereas ICI 79,939 showed no effect. The results are discussed with respect to their possible biological significance.

Alcohol Oxidoreductases↗
PubMed1975

[15-Hydroxyprostaglandin dehydrogenase from human placenta. 1. Isolation and characterization].

15-Hydroxyprostaglandin dehydrogenase was isolated from human term placenta up to a final purification of 380-fold. A spec. act. of 2000 mU/mg of protein was reached. The preparation was not homogeneous as judged by analytical disc electrophoresis. The enzyme could be stored in the presence of 50% glycerol and 10mM 2-mercaptoethanol without any loss of activity for at least one year. A distinct single protein band stained after discontinuous polyacrylamide gel electrophoresis was shown by enzymatic activity staining to correspond to 15-hydroxyprostaglandin dehydrogenase activity. Thus no evidence for the exitstence of isoenzymes was obtained. The protein in the final preparation steps showed neither alcohol dehydrogenase, NAD reductase, nor NADH oxidase activity, nor enzymatic conversion of prostaglandin or 15-oxoprostaglandin in the absence of NAD and NADH. No spontaneous reactions between NAD and prostaglandin or NADH and 15-oxoprostaglandin were detectable in the absence of the enzyme. Ethanol and glycerol slightly inhibited the reaction. Various buffers (Tris/HC1, potassium phosphate, HEPES, and triethanolamine) and salts (ammonium chloride, ammonium sulfate, potassium chloride, and sodium chloride) had different effects on the reaction rate. The pH profile of the reaction shows a plateau between pH 7.0 and 7.8 and a steep maximum at pH 9.5. A linear Arrhenius plot was obtained for the temperature dependence of the reaction from 20 to 37 degrees C. The molar activation enthalpy of the reaction was calculated to be 13.1 kcal/mole. The molecular weight of 15-hydroxyprostaglandin dehydrogenase was estimated to be 32000 -/+ 3000 by gel filtration on Sephadex G-150 in the presence of 10mM mercaptoethanol.

Alcohol Oxidoreductases↗
PubMed1974

The uptake and metabolism of (32-P)pyrophosphate by mouse calvaria in vitro.

In order to study the uptake and metabolism of PP(i) by bone, (32)PP(i) was added to the medium surrounding explanted mouse calvaria maintained in organ culture. Most of the PP(i) was hydrolysed during incubation, but there was a measurable entry of intact PP(i) into bone. When (32)P(i) was added to the medium, synthesis of PP(i) and organic phosphates from P(i) was observed in bone. There was no detectable passage of PP(i) from bone into the medium. These results are discussed in terms of two models of pyrophosphate hydrolysis and exchange. Some quantitative estimates about the fate of PP(i) in bone were made.

Animals↗