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At least 649 records · Page 36Linked to original sources
PubMed1972

Genetic control of enzyme induction in the -ketoadipate pathway of Pseudomonas putida: two-point crosses with a regulatory mutant strain.

Several mutant strains of Pseudomonas putida, selected on the basis of their inability to grow at the expense of benzoate, have been shown to be unable to form inducibly both muconate lactonizing enzyme and muconolactone isomerase. A secondary mutant strain derived from one of these pleiotropically negative strains forms these two enzymes and, in addition, catechol oxygenase in the absence of inducer. This constitutive mutant strain was used as a donor in transductionally mediated two-point crosses to determine the order of point mutations within the structural genes for muconate lactonizing enzyme and muconolactone isomerase (the catB and catC genes, respectively). The gene order conformed precisely with the one that has been established by deletion mapping.

Adipates↗
PubMed1982

Serum concentrations and enzyme induction in epileptic children treated with phenytoin and valproate.

In a group of 59 epileptic children treated with phenytoin (PHT) and valproate sodium (VPA), either alone or in combination, the following effects were studied: (1) the reciprocal effect on the serum levels of the two drugs, and (2) the enzyme-inducing effects of both drugs. VPA had no effect on PHT levels, but PHT significantly decreased VPA concentrations. PHT enhanced both gamma-glutamyltranspeptidase activity (gamma-GT) and D-glucaric acid excretion (GLA); these effects were potentiated by VPA. VPA alone did not affect gamma-GT, but significantly enhanced GLA.

Child↗
PubMed1977

Enzyme induction and renal function in man.

1. In a previous study in rats, an increased PAH clearance was found following chronic phenobarbitone administration. These results formed the basis for the present study in which fifteen healthy male volunteers were investigated and the parameters of liver microsomal enzyme activity and renal function were measured. 2. As parameters of liver microsomal enzyme activity, the antipyrine elimination in the plasma, the gamma-glutamyl-transpeptidase and the D-glucaric excretion in the urine were measured. Endogenous creatinine clearance, 51Cr-EDTA and 125I-Hippuran clearance were determined as measurements of renal function. 3. No correlation was found between any of the parameters of microsomal enzyme activity and renal function. 4. Of the fifteen volunteers, seven having a mean antipyrine half-life of 13.3 h were given antipyrine (500 mg) daily for 3 weeks. Afterwards all measurements of liver microsomal enzyme activity and renal function were repeated. The antipyrine half-life decreased to 8.5 h, while the antipyrine clearance was increased by about 56%. gamma-glutamyl-transpeptidase and D-glucaric acid were also significantly increased, while renal function remained unchanged. 5. Therefore, an increased PAH-clearance, as found in the rat, is not obtained in man following induction of liver microsomal enzyme activity.

Adult↗
PubMed1987

Angiotensin converting enzyme induction by cyclic AMP and analogues in cultured endothelial cells.

The role of cyclic AMP in regulating the production of angiotensin converting enzyme (ACE) was investigated using cultured bovine aortic endothelial cells. Addition of dibutyryl cAMP [Bu)2cAMP) at 100 microM increased the ACE activity to 126% of control (P less than 0.005). This effect was blocked by either actinomycin D (0.1 microgram/ml) or cycloheximide (1.7 microM) indicating that RNA as well as protein synthesis was required for induction of the enzyme. After addition of (Bu)2cAMP, a lag period of 8 h was observed before increased ACE activity was detected. The stable analogues, 8-bromo cAMP (100 microM) and N6-monobutyryl cAMP (100 microM) also increased ACE activity but cAMP (100 microM) and O2-monobutyryl cAMP (100 microM) had no effect, in keeping with their susceptibility to phosphodiesterase in this system. Sodium butyrate (100 microM) was also inactive. The effect of (Bu)2cAMP on ACE was still observed in the presence of a maximal dose of dexamethasone, indicating that (Bu)2cAMP stimulates by mechanism(s) independent of the previously observed action of glucocorticoids on these cells. The phosphodiesterase inhibitor IBMX caused a dose-related increase in ACE activity with a threshold at 30 microM (P less than 0.05) and produced a 4-fold increase above control at 1 mM IBMX.

1-Methyl-3-isobutylxanthine↗