[Renal cyst in childhood].
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Biomedical subjects
Publications and source records attributed to J Delgado.
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Selenate-resistant mutants of Candida utilis were isolated. They did not take up sulphate while incorporation of an organic sulphur source, such as L-methionine, was similar to the wild-type strain. They grew poorly on sulphate, sulphite and thiosulphate and, as expected, grew well on methionine. Sulphite reductase activities of the mutants were similar to the wild type strain. The properties of these mutants support the view of a common transport system for sulphate, sulphite and thiosulphate.
Sulphate uptake by Candida utilis follows Michaelis-Menten type kinetics characterized by a Km of 1.43 mM for sulphate. The process is unidirectional, pH, temperature and energy dependent. Molybdate, selenate, thiosulphate, chromate and sulphite are competitive inhibitors. Dithionite is a mixed-type inhibitor of sulphate uptake. If cells are pre-incubated with sulphate, sulphite, thiosulphate, dithionite or sulphide, sulphate uptake is severely blocked. Inhibition by endogenous sulphate, sulphite and thiosulphate was specific for sulphate uptake. Thus, incorporation of extracellular sulphate seems to be under the control of a heterogeneous pool of sulphur compounds. These results are discussed in connection with the regulation of sulphur amino acid biosynthesis in C. utilis.
Three of four patients whose cases fit the clinical description of psoas abscess proved on gallium imaging to have infection in the posterior pararenal space sparing the psoas muscle. This space provides a route for spread of infection connecting the spine, the anterior abdominal wall, the scrotum, the anterior thigh, and the gluteal region as demonstrated by the cases presented. Clinical differentiation between posterior pararenal space infection and psoas abscesses is difficult and CT studies may not demonstrate the process when the psoas space is not involved.
Incubation of cell-free extracts of C. utilis and its ethionine-resistant mutants with methionine, aspartate and alanine, and with various acceptor oxo-acids showed the presence of several transamination activities (Glu-Asp, Ala-Glu, Met-Glu, Met-Ala, Ala-Asp, but not Met-Asp). The lack of utilization of methionine by mec mutants appears to be due to a transport lesion.
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