Partial HPRT deficiency : heterozygotes exhibit one cell population in intact cell assays.
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Biomedical subjects
Publications and source records attributed to L Thompson.
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Altered leucyl-tRNA synthetase from a mammalian cell culture temperature-sensitive mutant, tsHl, was compared with enzyme from normal wild type Chinese hamster ovary cells. The mutant enzyme had a Km for leucine four times larger than that of wild type and enzyme levels 3-10% that of wild type. The presence of tRNA was necessary during in vitro heating of the mutant enzyme to allow expression of thermolability while the presence of tRNA protected wild type enzyme against thermal inactivation. The tsHl enzyme was stable when heated alone or in the presence of tRNA, leucine, and ATP simultaneously. The mutant's enzymes aminoacylated tRNALeu, tRNAVal, and tRNAIle with fidelity in vitro as determined by cochromatography of the amino-acyl-tRNA isoacceptors on RPC-5 reversed phase chromatography. The mutant failed to show any defect other than the direct formation of leucyl tRNALeu by leucyl-tRNA synthetase.
The "General Health Questionnaire" was used to assess the psychiatric morbidity among 365 consecutive attenders at a general practice and to compare this with a systematic random sample of 213 patients drawn from the lists of the same practice. Those attending a general practitioner are shown to be more psychiatrically disturbed than a random sample of the practice population, and this difference remains when those attending for psychological symptoms are discounted. Various social and demographic characteristics which distinguish between those who do and those who do not attend a doctor with a given set of psychological symptoms are described.
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A deficiency of adenine phosphoribosyltransferase (APRT) enzyme activity to approximately 40% of normal has been found in erythrocytes from a young woman aged 24 years, who had suffered from recurrent gouty arthritis since 11 years of age. She also demonstrated considerable, although asymptomatic, renal impairment with a creatinine clearance of one-third normal. Her father had suffered from gouty arthritis but had a normal APRT activity; he was obese, had a high purine intake and was a regular beer drinker. The patient's mother was asymptomatic with a normal serum urate concentration, but demonstrated a similar reduction in APRT activity to that of her daughter. Eleven other asymptomatic members of the family also demonstrated a similar reduction in APRT activity in erythrocyte lysates. The pattern of inheritance was consistent with autosomal transmission. Concentrations of phosphoribosylpyrophospate (PRPP) in erythrocytes were within normal limits both in the subjects with deficient, and in those with normal, APRT activity. Partial purification of APRT enzyme from erythrocytes of the index case did not reveal any difference from the normal enzyme as far as Michaelis constants, heat stability, or mobility in polyacrylamide gel was concerned. No primary abnormality of lipoprotein metabolism was demonstrated either in the propositus or in other members of her family. Study of urate metabolism in the propositus indicated that, although urate production was within the normal range in absolute terms, there was increased incorporation of glycine into produced urate, usually taken as one index of de novo urate production. Impaired renal excretion of urate was also shown. Although detailed study of urate metabolism has not been undertaken in other family members with APRT deficiency, no conclusive relationship has yet been demonstrated between APRT deficiency and disordered urate metabolism.
Drug usage review and inventory analysis data on the cephalosporin antibotics were presented by the pharmacy to a hospital pharmacy and therapeutics committee in an effort to promote rational use of these drugs and decrease drug costs. The committee recommended that cefazolin be the parenteral cephalosporin of choice. Cephalothin was placed on a limited formulary status for ophthamology patients and patients with renal impairment. Efforts by the committee to promote physician compliance with its recommendations are discussed.
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Both reaction-product localization and ferritin-coupled antibody studies have shown that alkaline phosphatase is evenly distributed throughout the peri-plasmic space of Escherichia coli and a marine pseudomonad. This space is not locally enlarged except in cases where plasmolysis has occurred.
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