Biomedical subjects
Publications and source records attributed to R C VALENTINE.
Cell-free filtrates of F(+) strains of Escherichia coli "inactivate" RNA phages. The active agents have been identified in the electron microscope as thin appendages called F-pili. Complexes of F-pili and phage may be easily assayed because of their retention by membrane filter pads. Calcium ion is required for formation of the complex.
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Bojanowski, R. (University of Illinois, Urbana), Elizabeth Gaudy, R. C. Valentine, and R. S. Wolfe. Oxamic transcarbamylase of Streptococcus allantoicus. J. Bacteriol. 87:75-80. 1964.-An improved colorimetric assay for carbamyl oxamate, which allows the precise measurement of the activity of oxamic transcarbamylase, has been developed. Activity is maximum over the pH range from 8.3 to 8.7. A cation requirement is satisfied by 2.5 x 10(-3)m Mg(++) or Mn(++). The equilibrium constant for the phosphorolysis of carbamyl oxamic acid is 1.6, corresponding to a negative free energy change of -285 cal per mole.
Valentine, R. C. (University of Illinois, Urbana), H. Drucker, and R. S. Wolfe. Glyoxylate fermentation by Streptococcus allantoicus. J. Bacteriol. 87:241-246. 1964.-Extracts of Streptococcus allantoicus were found to degrade glyoxylate, yielding tartronic semialdehyde and CO(2). Tartronic semialdehyde was prepared chemically, and its properties were compared with the enzymatic product: reduction by sodium borohydride yielded glycerate; heating at 100 C yielded glycolaldehyde and CO(2); autoxidation yielded mesoxalic semialdehyde; periodate oxidation yielded glyoxylate and a compound presumed to be formate. Tartronic semialdehyde reductase was present in extracts of S. allantoicus and in a species of Pseudomonas grown on allantoin. A scheme for the synthesis of acetate from glyoxylate by S. allantoicus is discussed.
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Valentine, R. C. (University of Illinois, Urbana) and R. S. Wolfe. Role of ferredoxin in the metabolism of molecular hydrogen. J. Bacteriol. 85:1114-1120. 1963.-The metabolism of molecular hydrogen by Clostridium pasteurianum, Micrococcus lactilyticus (Veillonella alcalescens), and several other anaerobic bacteria was studied. Oxidation of hydrogen, using several electron-accepting substrates including triphosphopyridine nucleotide, uric acid, xanthine, nitrite, and hydroxylamine, required ferredoxin in conjunction with hydrogenase. Evolution of hydrogen from pyruvate, alpha-ketoglutarate, hypoxanthine, and dithionite was mediated by ferredoxin. On the basis of these findings, a unitary hypothesis for biological hydrogen evolution is proposed in which ferredoxin plays a key role.
Wilder, Martin (University of Kansas, Lawrence), R. C. Valentine, and J. M. Akagi. Ferredoxin of Clostridium thermosaccharolyticum. J. Bacteriol. 86:861-865. 1963.-An electron-transferring agent has been isolated from Clostridium thermosaccharolyticum. This factor was found to participate as an electron carrier in the phosphoroclastic reaction of pyruvate, with the subsequent formation of acetyl phosphate and molecular hydrogen. It can be employed interchangeably with the ferredoxin of C. pasteurianum in various reactions. Thermal-stability studies indicated that this factor from C. thermosaccharolyticum was comparatively more heat-resistant than the carrier obtained from C. pasteurianum. It was concluded that this carrier was ferredoxin or a ferredoxin-like substance.
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