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Biomedical subjects

H Meyer

Publications and source records attributed to H Meyer.

At least 469 records · Page 26Linked to original sources
PubMed1979

[Examination of the retest reliability of the findings of the first psychopathological examination (AMP system)].

80 inpatients were interviewed two times by the same rate during 24 h. Using Kappa, the retest reliability of the following parts of the psychopathological findings was determined: (1) aspects of the interview (median 0.54); (2) AMP symptoms (median 0.72); (3) AMP syndromes (median 0.79); (4) clinical syndromes (median 0.77), and (5) nosologic diagnoses (median 0.93). Based on structured rating of the psychopathological symptoms, a good retest reliability was found.

Adolescent↗
PubMed1979

[The influence of the ester function on the vasodilating activity of 1,4-dihydro-2,6-dimethyl-4-nitrophenyl-pyridine-3,5-dicarboxylates (author's transl)].

In the series of 1,4-dihydro-2,6-dimethyl-4-nitrophenyl-pyridine-3,5-dicarboxylates the vasodilating action (increase of O2-saturation in the coronary sinus of the dog) is found to be dependent on the position of the nitro function (ortho and meta superior to para) and on the nature of the ester group. One representative, niludipin (BAY a 7168, No. 17; bis(2-propoxyethyl)-1,4-dihydro-2,6-dimethyl-4-(3-nitrophenyl)-3,5-pyridinedicarboxylate) was selected for further pharmacological studies.

Animals↗
PubMed1978

A photochemically induced dynamic nuclear polarization study of pancreatic phospholipase A2. NMR assignment of some aromatic residues.

Application of the photochemically induced dynamic nuclear polarization technique to porcine pancreatic phospholipase A2 and its precursor resulted in the observation of nuclear spin polarization for the single tryptophan and 2 tyrosine residues. Using selectively nitrated enzymes, the tyrosine resonances could be assigned to residues 69 and 123. Both tryptophan-3 and tyrosine-69 are of particular interest because they are part of the lipid binding site.

Binding Sites↗
PubMed1978

Acyl-coenzyme A carboxylase of the free-living nematode Turbatrix aceti. 1. Its isolation and molecular characteristics.

A biotin containing enzyme which carboxylates acetyl-CoA has been isolated from the nematode Turbatrix aceti and purified to homogeneity as judged by the criteria of polyacrylamide gel electrophoresis and ultracentrifugation. The enzyme has a sedimentation coefficient of 18.0 S and a molecular weight of 667 000. It is composed of four protomers having a molecular weight of 140 000 each. Each protomer, in turn, consists of two distinct polypeptide chains (molecular weights 82 000 and 58 000) and one biotinyl prosthetic group which is linked to the 82 000 peptide. The amino acid composition of the nematode carboxylase has also been determined.

Acetyl Coenzyme A↗
PubMed1978

Acyl-coenzyme A carboxylase of the free-living nematode Turbatrix aceti. 2. Its catalytic properties and activation by monovalent cations.

A highly purified acyl-CoA carboxylase from the nametode Turbatrix aceti catalyzes the ATP, Mg2+, and HCO3- dependent alpha-carboxylation of acetyl-CoA, propionyl-CoA, and butyryl-CoA at the respective rates of 6.8, 39.7, and 9.1 mumol per min per mg. The enzyme is inhibited by avidin and sulfhydryl reagents. It is activated up to 30-fold by the monovalent cations K+, Rb+, Cs+, or NH4+, with the apparent activation constants of 11.0, 4.1, 10.0, and 6.7 mM, respectively. In the presence of K+, the apparent Km for ATP increases 5-fold, and the Km for HCO3- decreases 4-fold, whereas the Km for propionyl-CoA remains constant. Of the partial reactions, the ATP-32P exchange reaction and the carboxylation of free biotin have a nearly absolute requirement for K+. By contrast, the [14C]acetyl-CoA-malonyl-CoA exchange reaction proceeds without K+ at 80% of its maximum rate. The data indicate that K+ primarily stimulates the first half of the carboxylation reaction, i.e., the ATP-dependent carboxylation of the biotinyl residue.

Animals↗
PubMed1977

[Bacterial flora and nitrite production in the stomach after gastroenterostomy. Experimental aspects of the pathogenesis of carcinoma in the operated stomach (author's transl)].

A gastroenterostomy without enteroanastomosis leads to a change in the bacterial flora of the stomach, where-by in particular the proportion of nitrite-decomposing bacteria, is enhanced. This results in an increase of nitrite concentration in the gastric fluid, which may possibly be accompanied by an augmented production of carcinogenic nitrosoamine. This latter aspect is considered with respect to the origin of carcinoma in the operated stomach. Since the reported changes will be largely prevented by a Roux-Y-gastroenterostomy, this should be taken into consideration for reconstruction of the alimentary tract after gastric surgery.

Animals↗