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Biomedical subjects

H Frischer

Publications and source records attributed to H Frischer.

54 records · Page 3Linked to original sources
PubMed1973

NAD(P) glycohydrolase deficiency in human erythrocytes and alteration of cytosol NADH-methemoglobin diaphorase by membrane NAD-glycohydrolase activity.

Erythrocytic NADH methemoglobin diaphorase acquires NADH-dichlorophenolindophenol diaphorase activity when enzyme-associated NAD is removed. This transformation is reversible and can be mediated by membrane NAD glycohydrolase (EC 3.2.2.5) in hemolysates as well as in intact cells exposed to hydrogen peroxide. It is abolished either in NADH methemoglobin diaphorase deficiency or in NAD(P) glycohydrolase (EC 3.2.2.6) deficiency which is common in Afro-American but not in European-American adults. Activities of erythrocytic NADP glycohydrolase and NAD glycohydrolase appear to depend on a single membrane enzyme.

Cell Membrane↗
PubMed1968

Gametocytocidal and sporontocidal effects of primaquine and of sulfadiazine with pyrimethamine in a chloroquine-resistant strain of Plasmodium falciparum.

Studies with 3 volunteers were conducted to determine the effects of a combination of sulfadiazine and pyrimethamine and the effects of primaquine upon mature gametocytes of a strain of chloroquine-resistant Plasmodium falciparum-the Malayan (Camp.) strain. One volunteer was treated with sulfadiazine and pyrimethamine; two other volunteers each received a single dose of 45 mg of primaquine base. The combination of sulfadiazine and pyrimethamine, although active against blood schizonts, did not exert a marked sporontocidal effect against the Malayan (Camp.) strain. In sharp contrast, primaquine, although not effective as a blood schizontocide, exerted a marked gametocytocidal and sporontocidal effect against this strain.The findings emphasize the need for further studies of the sporontocidal and gametocytocidal effects of drugs, particularly primaquine, against chloroquine-resistant strains of P. falciparum and suggest that primaquine may come to play an important role in preventing the transmission of such strains.

Adult↗
PubMed1967

Characterization of enterobacteria by starch-gel electrophoresis of glucose-6-phosphate dehydrogenase and phosphogluconate dehydrogenase.

Specific activities and electrophoretic mobilities of glucose-6-phosphate dehydrogenase and phosphogluconate dehydrogenase were determined in 38 isolates of the family Enterobacteriaceae and in 10 isolates of the related Pasteurella. The deficiency of glucose-6-phosphate dehydrogenase in P. pestis was verified. Enzymes obtained from different strains of the same species exhibited an unexpected degree of heterogeneity. For example, 8 and 11 apparent variants of glucose-6-phosphate dehydrogenase and phosphogluconate dehydrogenase, respectively, were found in 14 strains of Escherichia coli. Although similar frequencies of heterogeneity were noted in 7 strains of P. pseudotuberculosis, 5 species of Shigella, and 8 species of Salmonella, differences in mobility were generally small in comparison with those observed between strains of E. coli. Values obtained for the pasteurellae, shigellae, and salmonellae, thus fell within narrow ranges that may prove typical for the genera. However, most of these ranges, as well as many values observed for single species of other genera, were overlapped by the wide range recorded for E. coli. The significance of this observation was discussed with respect to the relative age and taxonomic position of the organisms in question. The method could be used to distinguish between most wild-type strains of the same species and should thus facilitate investigations of genetic transfer and epidemiology.

Electrophoresis↗