Quality, the patient's charter, and primary care.
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Biomedical subjects
Publications and source records attributed to C W Parr.
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1. Soluble extracts from different strains of Trypanosoma evansi were compared by several analytical procedures. 2. No isoenzymic differences were detected. 3. Some clear intraspecies differences in protein isoelectric points, in polypeptide sizes and in free amino acid contents were found.
1. The phosphoglucose isomerases (PGI's) of the bloodstream forms of Trypanosoma brucei and T. vivax have been purified some 150-fold, using cellulose ion-exchange chromatography, gel filtration and isoelectric focussing. 2. The two trypanosome enzymes showed many similarities in kinetic properties, but differed from each other somewhat in thermal stability and in isoelectric point. 3. Both trypanosome enzymes differ from PGI's from other sources in having a higher Ki for the competitive inhibitor 6-phosphogluconate.
Human erythrocyte glyoxalase I has been subjected to starch gel electrophoresis, and its isoenzymatic forms have been visualized by a new positive staining procedure. The enzyme exhibits polymorphism and holds promise as a useful new genetic marker.
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161 inhabitants of the Seychelle Islands have been examined for blood group, serum protein, and red cell enzyme polymorphisms. The gene frequency data obtained from this survey supports the anthropological view that the present-day Creole-speaking inhabitants of the Seychelle Islands result from a admixture of African and European stock.
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An autosomally inherited variant of the rabbit enzyme phosphoglucose isomerase that differs both electrophoretically and kinetically from the usual (wild-type) rabbit enzyme has been investigated. Animals homozygous for this character have an isomerase with considerably decreased activity (in the erythrocytes), an increased K(m) for fructose 6-phosphate, an increased K(i) for 6-phosphogluconate and a decreased stability towards heat and urea. The variant enzyme has been demonstrated in erythrocytes, leucocytes and tissues from the affected rabbits. The kinetic evidence suggests that the mutation present in the variant enzyme affects a histidine residue.
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