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Biomedical subjects

B Bakay

Publications and source records attributed to B Bakay.

At least 55 records · Page 3Linked to original sources
PubMed1975

Continuous monitoring of radioactivity of effluent from a high-speed amino acid analyzer, with a new system of sample segmentation.

Radioactivity in the effluents from high-speed liquid chromatographic analyzers was continuously measured by use of a new sample segmentation system. To achieve highest counting efficiency, the column effluents were mixed with scintillation fluid carrying small segments of semisolid, resillient spacer. After passing through a mixer, the mixture was passed through a hollow-tube flow cell mounted in a liquid scintillation spectrometer. Because the added spacer acts like a continuous series of pistons, it unifies flow rate at center and walls of the conduit and so decreases sample carryover. This system was applied to measurement of radioactivity in the effluent of a high-speed amino acid analyzer, in which some amino acids emerge at 30-s intervals. The resulting profiles were as well resolved as were the ninhydrin-color profiles. Counting efficiencies for tritium and carbon- 14 were comparable to those obtained by static counting in vials.

Amino Acids↗
PubMed1973

Restoration of hypoxanthine phosphoribosyl transferase activity in mouse 1R cells after fusion with chick-embryo fibroblasts.

Fusion of the 1R mouse cell, which lacks activity of hypoxanthine phosphoribosyl transferase (EC 2.4.2.8), with chick-embryo fibroblasts yielded progeny cells that survived in hypoxanthine-aminopterin-thymidine selective medium. This property and the failure of the progeny to survive in 8-azaguanine indicated that hypoxanthine phosphoribosyl transferase activity was present. Electrophoretic analysis revealed that the enzyme was of mouse, not chick, origin. These observations are consistent with the operation of a regulator gene responsible for the absence of hypoxanthine phosphoribosyl-transferase activity in the 1R cell and its presence in the progeny.

Adenine↗
PubMed1973

Reexpression of the rat hypoxanthine phosphoribosyltransferase gene in rat-human hybrids.

Fusion of hypoxanthine phosphoribosyltransferase (HPRT)(-) rat hepatoma cells with HPRT(+) human fibroblasts yielded hybrid clones that grew in HAT selective medium and contained all the rat chromosomes and one to nine human chromosomes. Among the retained chromosomes was the human X chromosome. In all clones backselected in medium containing 8-azaguanine, human X chromosome was absent. Electrophoretic analysis revealed that, without exception, hybrid clones growing in HAT medium had an active HPRT enzyme, either human or rat, or both. When these clones were backselected in 8-azaguanine, they did not show HPRT enzyme activity. Hybrids that contained the human X chromosome also had human glucose-6-phosphate dehydrogenase. The observed reexpression of rat HPRT in hybrid cells derived from HPRT(-) rat cells suggests that a genetic factor from the human cell determined the expression of the rat structural gene for HPRT.

Adenine↗
PubMed1972

Activation of variants of hypoxanthine-guanine phosphoribosyl transferase by the normal enzyme.

Deficient hypoxanthine-guanine phosphoribosyl transferase (HGPRT; EC 2.4.2.8) enzymes from erythrocytes of patients with hyperuricemia and with the Lesch-Nyhan syndrome migrate 15% faster in polyacrylamide gel disc electrophoresis than the normal enzyme. A half-sister of two males with partial deficiency, who had 34% of normal HGPRT activity in her erythrocytes, yielded profiles containing two distinct zones of activity; one corresponded to the enzyme found in normal individuals and one to the variant of her half-brothers. However, in her profile her variant enzyme showed notably greater activity than that observed in her half-brothers. This increase was due to an activation of the variant by normal enzyme. Electrophoresis of mixtures of normal enzyme with partially deficient enzymes from patients with hyperuricemia and with the Lesch-Nyhan syndrome also led to activation of deficient HGPRT variants by normal enzymes. Deficient variants were also activated by normal enzyme on filtration through Sephadex G-25. Experiments in which deficient variant enzymes were activated with purified normal enzyme labeled with (125)I indicated that deficient enzymes incorporate components of the normal enzyme. No such activation of deficient enzymes was ever obtained when mixtures of deficient and normal enzymes were put together in a test tube.

Athetosis↗
PubMed1970

Hemizygous expression of glucose-6-phosphate dehydrogenase in erythrocytes of heterozygotes for the Lesch-Nyhan syndrome.

In women heterozygous for hypoxanthine guanine phosphoribosyl trasferase deficiency, the activity of this enzyme in the erythrocyte is usually normal. In a key kindred two such obligate heterozygotes were also heterozygous for glucose-6-phosphate dehydrogenase types A and B. The AB genotype was confirmed in one by assay of skin fibroblasts. Erythrocytes were exclusively of type B. These observations suggest the clonal origin of the hematopoietic system in these women from a primordial cell line with a single active X chromosome.

Cell Line↗