Biomedical subjects
Publications and source records attributed to M Orlowski.
The drug chlorpromazine inhibits respiration in several gram-negative bacteria. The enzymes glucose-6-phosphogluconate dehydrogenase and 6-phosphogluconate dehydrogenase from these microorganisms are not affected by the drug.
The process of sporulation was studied in Bacillus stearothermophilus. A medium is described that supports good growth and sporulation of the organism. In this medium, which contains glucose, salts, and amino acids, acetate starts to accumulate before any of the glucose is catabolized. Enzymes of the tricarboxylic acid cycle are present at all times during growth and sporulation and are found in dormant spores. As the glucose in the culture is consumed, acetate rapidly increases and the pH of the medium drops. The acetate rapidly disappears during sporulation and the pH rises. Dipicolinic acid appears during sporulation and several key-enzyme activities fluctuate in a characteristic pattern.
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A fraction containing capillaries and rich in gamma-glutamyl transpeptidase was isolated from homogenates of bovine brain cortex by density gradient centrifugation. The enzyme was localized in the endothelial cells by a histochemical procedure. gamma-Glutantyl transpeptidase may function in the transfer of some amino acids across the blood-brain barrier.
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The inactivation of isocitrate lyase which occurs during late stages of myxospore formation in Myxococcus xanthus was studied. Several findings are reported. (i) Protein synthesis is required over a specific time interval in order for isocitrate lyase inactivation to occur at a later time. (ii) Metabolic energy is required at all times during myxospore development if the inactivation is to occur. (iii) It was possible to inhibit protein turnover to a considerable extent without affecting the net loss in isocitrate lyase activity.
The following enzymatic activities were demonstrated in Myxococcus xanthus during growth and myxospore formation: l-alanine dehydrogenase (EC 1.4.1.1), l-glutamic acid dehydrogenase (EC 1.4.1.2), glycine dehydrogenase (EC 1.4.1.5), l-glutamic glyoxylate aminotransferase (EC 2.6.1.4), and l-alanine glyoxylate aminotransferase (EC 2.6.1.12).
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L-2-Imidazolidone-4-carboxylic acid is an effective competitive inhibitor of the reaction catalyzed by 5-oxoprolinase, in which 5-oxo-L-proline (L-pyroglutamic acid, L-2-pyrrolidone-5-carboxylic acid, L-5-oxopyrrolidine-2-carboxylic acid) is converted to L-glutamate, with concomitant cleavage of ATP to ADP and orthophosphate. L-2-Imidazolidone-4-carboxylate decreased the rate of metabolism of 5-oxo-L-[(14)C]proline to (14)CO(2) by rat-kidney slices but had no effect on the metabolism of [(14)C]glutamate. Mice injected with L-2-imidazolidone-4-carboxylate exhibited greatly reduced ability to metabolize 5-oxo-L-proline, but metabolized glutamate at an essentially normal rate. The findings provide an approach to an animal model for the human condition 5-oxoprolinuria, in which there is apparently a deficiency of renal 5-oxoprolinase activity. The evidence indicates that 5-oxoproline is a normal metabolite.
Activities of the glyoxylate cycle enzymes isocitrate lyase (EC 4.1.3.1) and malate synthase (EC 4.1.3.2) were assayed in extracts prepared at different stages of myxospore formation in liquid cultures of Myxococcus xanthus. Activities of both enzymes attained peak values during conversion of rods to spheres. Isocitrate lyase activity decreased after reaching its peak value. Malate synthase activity also declined but at a much slower rate. The loss of isocitrate lyase activity could be prevented by the addition of chloramphenicol to cultures early in myxospore formation (during the initial rise in enzyme activity), but not by such addition at later stages of myxospore formation. The increase in glyoxylate cycle enzymes was not observed in a mutant unable to form myxospores in liquid culture under conditions suitable for morphological conversion of the wild type, or in wild-type cells incubated in the absence of an inducer for myxospore formation. It is concluded that the changes in the glyoxylate cycle enzymes represent regulatory phenomena associated with the development of the myxospore.
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A new enzyme, 5-oxoprolinase, was found in rat kidney and in several other tissues; it catalyzes the conversion of 5-oxo-L-proline (L-5-oxo-pyrrolidine-2-carboxylic acid, L-2-pyrrolidone-5-carboxylic acid, L-pyroglutamic acid) to L-glutamic acid, with concomitant stoichiometric cleavage of ATP to ADP and orthophosphate. The reaction catalyzed by 5-oxoprolinase, in which 5-oxoproline formed from gamma-glutamyl amino acids by the action of gamma-glutamylcyclotransferase is converted to glutamate, appears to function in the gamma-glutamyl cycle. 5-Oxoprolinase requires Mg(++) (or Mn(++)) and K(+) (or NH(4) (+)) for activity. The equilibrium is markedly in favor of glutamate formation at pH 7.8.
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