Biomedical subjects
K Pfister
Publications and source records attributed to K Pfister.
Syncatalytic conformational changes in aspartate aminotransferase determined by hydrogen-deuterium exchange.
Catalysis-linked conformational transitions of aspartate aminotransferase (cytosolic isoenzyme from pig heart; L-aspartate:2-oxoglutarate aminotransferase, EC 2.6.1.1) have been probed by infrared spectrophotometric measurement of hydrogen-deuterium exchange. In the unliganded pyridoxal form of the enzyme at pH 6.0 and 20 degrees, 43% of the total 411 peptide hydrogens per subunit exchange within the first 10 min. An additional 9% exchange slowly in the following time period to 360 min. A quite similar exchange curve is obtained with the pyridoxamine form of the enzyme, indicating close correspondence in conformation of both unliganded forms of the enzyme. Formation of a nonproductive adsorption complex of the pyridoxal enzyme with 2-oxoglutarate or of the pyridoxamine enzyme with glutamate alters the exchange characteristics only slightly. In contrast, the formation of an equilibrium mixture of the covalent transamination intermediates, which occurs in the silultaneous presence of the amino acid and the keto acid substrate, results in a marked retardation of hydrogen exchange, reflecting a substantial tightening of the structure of the enzyme. The exchange reactions of at least 26 peptide hydrogens per subunit (6% of the total) are retarded by a factor of 6 on the average. The occurrence of such syncatalytic conformational changes reflects energetic coupling of the covalency changes at the active site with conformational changes of the macromolecular protein matrix that may contribute to optimizing the free energy profile of enzymic transamination.
[Epizootological views on the occurrence of Psoroptes mange and other ectoparasites in the sheep in the canton Bern].
Explore the source record for details and available documents.
[Results of an attempt at therapy of intestinal helminthiasis in fattening lambs under conditions of general practice].
Explore the source record for details and available documents.
[Ovine cysticercosis and its relationship to tape-worm infestation in the dog].
Explore the source record for details and available documents.
[Structure and function of enzymes. A brief introduction].
Explore the source record for details and available documents.
Synthesis of alpha-methyl-DLg-glutathione.
Explore the source record for details and available documents.
Effect of strategic gastrointestinal nematode control on faecal egg count in traditional West African cattle.
This paper reports on the effect of strategic anthelmintic treatments and other determinants on faecal egg counts (FEC) of Trichostrongyles in N'Dama cattle of a west African village. Initially, 527 animals from 13 private N'Dama cattle herds were monitored in a longitudinal study from October 1989 to December 1994. Each herd was stratified by age and animals were sequentially allocated to two groups with similar age distributions. One group received a single anthelmintic treatment of fenbendazole (7.5 mg/kg BW), in October 1989 (n = 250), whereas the other group remained untreated (n = 277) throughout the study. In the next rainy season (June to October), the treated animals were treated twice (in July and September). The same treatment schedule was used in the subsequent rainy seasons until December 1994. Biannual anthelmintic treatments decreased the level of FEC between 31% (late dry season) and 57% (rainy season), when compared to untreated controls. The highest levels of FEC were found during the rainy season from June to October. FEC levels decreased until 4 years of age, after which they remained on a constant low level. The variability of returns to anthelmintic treatments between herds did not seem to be influenced by FEC at the herd level. The financial evaluation of anthelmintic interventions cannot be predicted from FEC and must necessarily rely on the direct monitoring of livestock productivity parameters.
[125I]azido-ioxynil labels Val249 of the photosystem II D-1 reaction center protein.
Azido-ioxynil (3.5-diiodo-2-azido-4-hydroxy-benzonitrile) is a potent photosystem II inhibitor (pI50-value 7.38) and as effective as the parent compound ioxynil itself. [125I]azido-ioxynil exhibits specific binding to isolated thylakoids with a binding constant Kb = 7.14. Upon UV-illumination it binds covalently to thylakoids or photosystem II particles. It labels predominantly the 32 kDa D-1 photosystem II reaction center protein. A 41 kDa protein is only tagged in trace amounts. After proteolytic treatment of labeled D-1 protein with Staphylococcus aureus V8-protease two major and two minor fragments are obtained. Automated gas phase sequencing of a 7 kDa cleavage peptide revealed that Val249 is the primary target of azido-ioxynil binding. Compared to urea type herbicides, this places the ioxynil binding site in a different environment of the D-1 photosystem II protein.