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P J VANDEMARK

Publications and source records attributed to P J VANDEMARK.

14 recordsLinked to original sources
PubMed1965

NATURE OF BUTYRATE OXIDATION BY MYCOPLASMA HOMINIS.

VanDemark, P. J. (Cornell University, Ithaca, N.Y.), and P. F. Smith. Nature of butyrate oxidation by Mycoplasma hominis. J. Bacteriol. 89:373-377. 1965.-Cell-free extracts of butyrate - grown Mycoplasma hominis strain O7, though lacking thiokinase activity on butyric acid, were found to activate butyrate via an acetyl-butyric thiophorase. These extracts also contained an aceto-coenzyme A (CoA) kinase, a butyryl-CoA dehydrogenase, a crotonase, a reduced nicotinamide adenine dinucleotide-specific beta-hydroxybutyryl-CoA dehydrogenase, and a thiolase. Thiolase activity was stimulated by the addition of magnesium ions. The presence of these enzyme activities in this Mycoplasma species supports the hypothesis that a fatty acid oxidation represents an energy source for the nonfermentative pleuropneumonia-like organisms.

3-Hydroxyacyl CoA Dehydrogenases↗
PubMed1964

RESPIRATORY PATHWAYS IN THE MYCOPLASMA. II. PATHWAY OF ELECTRON TRANSPORT DURING OXIDATION OF REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE BY MYCOPLASMA HOMINIS.

VanDemark, P. J. (University of South Dakota, Vermillion), and P. F. Smith. Respiratory pathways in the Mycoplasma. II. Pathway of electron transport during oxidation of reduced nicotinamide adenine dinucleotide by Mycoplasma hominis. J. Bacteriol. 88:122-129. 1964.-Unlike the flavin-terminated respiratory pathway of the fermentative Mycoplasma, the respiratory chain of the nonfermentative M. hominis strain 07 appears to be more complex, involving quinones and cytochromes in addition to flavins. In addition to reduction by reduced nicotine adenine dinucleotide (NADH) and reduced nicotine adenine dinucleotide phosphate, nonpyridine nucleotide-linked reduction of the respiratory chain of this organism occurred with succinate, lactate, and short-chained acyl coenzyme A derivatives as electron donors. Enzymes catalyzing the oxidation of NADH included an NADH oxidase, a diaphorase, a quinone reductase, and a cytochrome c reductase. The oxidation of NADH was sensitive to a variety of inhibitors, including 10(-4)m Atabrine, 10(-3)m sodium amytal, 10(-5)mp-chloromercuribenzoate, 10(-4)m antimycin A, and 10(-4)m potassium cyanide. The oxidase was resolved by the addition of 5% trichloroacetic acid and reactivated by the addition of flavin adenine dinucleotide but not flavin mononucleotide. The M. hominis sonic extract contained an NADH-coenzyme Q reductase. The oxidation of NADH was stimulated by the addition of either menadione or vitamin K(2) (C(35)). The oxidase was inactivated by extraction with ether or irradiation at 360 mmu. The ether-inactivated enzyme was partially reactivated by the addition of "lipid" extract of the enzyme and coenzyme Q(6). Difference spectra of the cell extracts revealed the presence of "b" and "a" type cytochromes. These cell extracts were found to contain a cyanide-and azide-sensitive cytochrome oxidase and catalase.

Catalase↗
PubMed1964

EVIDENCE FOR A TRICARBOXYLIC ACID CYCLE IN MYCOPLASMA HOMINIS.

VanDemark, P. J. (Cornell University, Ithaca, N.Y.), and P. F. Smith. Evidence for a tricarboxylic acid cycle in Mycoplasma hominis. J. Bacteriol. 88:1602-1607. 1964.-Resting cells of acetate-grown Mycoplasma hominis strain 07 oxidized the various intermediates of the tricarboxylic and glyoxylate cycles, with the exception of sodium citrate and glyoxylate. Extracts of these cells possessed isocitric dehydrogenase, isocitratase, alpha-ketoglutaric dehydrogenase, succinic dehydrogenase, fumarase, malic dehydrogenase, citratase, and acetyl coenzyme A kinase activities. With the assay conditions employed, condensing enzyme, malate synthetase, and phosphotransacetylase activities were negligible. Incubation of sodium acetate-2-C(14) with the various intermediates of the tricarboxylic acid cycle in the presence of cell-free extracts resulted in exchange of the isotope with these compounds as well as the formation of other labeled intermediates of the tricarboxylic acid cycle. Oxidation of sodium acetate-2-C(14) alone resulted in the formation of labeled succinate, fumarate, and malate.

Acetates↗
PubMed1963

RESPIRATORY PATHWAYS IN THE MYCOPLASMA. I. LACTATE OXIDATION BY MYCOPLASMA GALLISEPTICUM.

Smith, S. L. (Cornell University, Ithaca, N.Y.), P. J. Van Demark, and J. Fabricant. Respiratory pathways in the Mycoplasma. I. Lactate oxidation by Mycoplasma gallisepticum. J. Bacteriol. 86:893-897. 1963.-Resting cells of Mycoplasma gallisepticum 293 required the addition of nicotinamide adenine dinucleotide, thiamine pyrophosphate, and flavine mononucleotide for the maximal rate of sodium lactate oxidation. Inhibitor studies, as well as spectrophotometric and chemical assays, indicate that the pathway of electron transport to oxygen during lactate oxidation does not involve heme catalysts, and is mediated by flavin-linked enzyme systems. The presence of reduced nicotinamide adenine dinucleotide-specific lactic dehydrogenase, menadione reductase, ferricyanide reductase, and reduced nicotinamide adenine dinucleotide oxidase activities was detected in cell-free extracts. No cytochrome c reductase or reduced nicotinamide adenine dinucleotide peroxidase activity was detected in these extracts.

Adenine Nucleotides↗
PubMed1961

Nutrition of Streptococcus bovis in relation to dextran formation.

Barnes, Isabel J. (Cornell University, Ithaca, N. Y.), H. W. Seeley, and P. J. VanDeMark. Nutrition of Streptococcus bovis in relation to dextran formation. J. Bacteriol. 82:85-93. 1961.-Three nutritional types of Streptococcus bovis were encountered. Minimal media for their growth are described. Transferable growth in defined media was always accompanied by dextran production and the nutrition for dextran production could not be distinguished from the minimal nutritional requirements of the organism for growth. Measurable, free CO(2) was evolved from a complex medium during the growth of S. bovis. Several compounds were found to replace partially the CO(2) requirement of the species. When fractured cell preparations containing S. bovis dextran were employed as antigens, rabbits failed to yield sera which would precipitate S. bovis or leuconostoc dextrans.

Dextrans↗