Showing papers in "Biochemical Journal in 1953"

The colorimetric estimation of formaldehyde by means of the Hantzsch reaction

Abstract: Bonnichsen, R. K. (1947). Arch. Biochem. 12, 83. Dalgliesh, C. E. (1951). Quart. Rev. chem. Soc., Lond., 5,227. Daigliesh, C. E. (1952). Biochem. J. 52, 3. Eckert, H. W. (1943). J. biol. Chem. 148, 205. Elliott, K. A. C. (1932a). Biochem. J. 26, 10. Elliott, K. A. C. (1932b). Biochem. J. 26, 1281. Galston, A. W. (1949). Plant Phy8iol. 24, 577. Gordon, S. A. & Nieva, F. S. (1949). Arch. Biochem. 20,356. Gustafson, F. G. (1949). Science, 110, 279. Happold, F. C. (1950). Advanc. Enzymol. 10, 51. Henderson, J. M. & Bonner, J. (1952). Amer. J. Bot. 39, 444. Horn, M. J. & Jones, D. B. (1945). J. biol. Chem. 157, 153. Keilin, D. & Hartree, E. F. (1951). Biochem. J. 49, 88. Kenten, R. H. & Mann, P. J. G. (1952). Biochem. J. 50,360. Knox, W. E. (1951). Brit. J. exp. Path. 32, 462. Knox, W. E. & Mehler, A. H. (1950). J. biol. Chem. 187,419. Makino, K., Satoh, K., Fujiki, T. & Kawaguchi, K. (1952). Nature, Lond., 170, 977. Morton, R. K. (1950). Nature, Lond., 166, 1092. Nason, A. (1950). Amer. J. Bot. 37, 612. Proctor, B. E. & Bhatia, D. S. (1953). Biochem. J. 53, 1. Reichstein, T. (1932). Helv. chim. acta, 15, 1110. Singer, T. P. & Kearney, E. B. (1950). Arch. Biochem. 29, 190. Sizer, I. W. (1947). Fed. Proc. 6, 202. Stanier, R. Y. & Tsuchida, M. (1949). J. Bact. 58, 45. Tang, Y. W. & Bonner, J. (1947). Arch. Biochem. 13, 11. Teas, H. J. & Anderson, E. G. (1951). Proc. nat. Acad. Sci., Wash., 37, 645. Weil, L., Gordon, N. G. & Buchert, A. R. (1951). Arch. Biochem. 33, 90. Wildman, S. G., Ferm, M. G. & Bonner, J. (1947). Arch. Biochem. 13, 131. Wildman, S. G. & Muir, R. M. (1949). Plant Physiol. 24, 84.

Further studies on the properties and assay of glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase of rat liver.

Abstract: Renewed interest in the direct oxidative pathway of glucose 6-phosphate metabolism during the last few years has revealed that this pathway is by no means restricted to erythrocytes, yeast and microorganisms. The triphosphopyridine-nucleotide(TPN)-specific glucose 6-phosphate and 6-phosphogluconate dehydrogenases are also widely distributed in mammalian tissues (Dickens & Glock, 1950, 1951; Horecker & Smyrniotis, 1951), in a variety of lower plants and animals (Cohen, 1950) and also in higher plants (Conn & Vennesland, 1951; Gibbs, 1952). The significance of this pathway in animal tissues, its physiological control and the relative importance of the direct oxidative and glycolytic routes of carbohydrate metabolism are still, however, chiefly matters of conjecture. An essential preliminary step to such an investigation is to devise a satisfactory procedure for the assay of glucose 6-phosphate and 6-phosphogluconate dehydrogenases in animal tissues and it was with this object in view that the present work was undertaken.

The assimilation of amino-acids by bacteria. XV. Actions of antibiotics on nucleic acid and protein synthesis in Staphylococcus aureus.

Abstract: In previous papers of this series, experimental conditions have been described which will enable the following processes to be studied in washed suspensions of Staphylococcus aureus (Micrococcus pyogenes var. aureus): internal accumulation of free glutamic acid (Gale, 1947 a, b), extracellular accumulation of peptides containing glutamic acid (Gale & Van Halteren, 1951), accumulation of combined glutamic acid within the cells (Gale, 1951 b) and synthesis of protein and nucleic acid (Gale & Folkes, 1953). Aureomycin and chloramphenicol inhibit the increase of cellular combined glutamate at lower concentrations than those necessary to prevent the accumulation of free glutamic acid within the cells, whereas sodium azide, 2:4-dinitrophenol and 8-hydroxyquinoline affect these processes to approximately the same extent (Gale & Paine, 1951). Penicillin and bacitracin have no effect upon the accumulation of free or combined glutamic acid in washed suspensions of cells, but if either of these antibiotics is added to the growth medium an hour before harvesting, the resulting cells are unable to accumulate either free or combined glutamic acid (Gale & Taylor, 1947; Gale & Paine, 1951; Paine, 1951). Hotchkiss (1950) has described a disorganization of protein synthesis by penicillin which results, under the conditions of his experiments, in extracellular accumulation of peptides when Staph. aureus is incubated with amino-acid mixtures. Mitchell & Moyle (1951) followed the nucleic acid content of Staph. aureus during normal growth and in the presence of penicillin. During the normal phase of accelerated growth they found that nucleic acid reproduced more rapidly than cell dry weight, suggesting that nucleic acid controlled the rate of cell synthesis. A disturbance of nucleic acid metabolism occurred in the presence ofpenicillin and was accompanied by an intracellular accumulation of extractable nucleotides. Krampitz & Werkman (1947) and Gros & Macheboeuf (1948a, b) have previously described inhibitions of nucleic acid metabolism in bacterial cells by high concentrations of penicillin, while Gros, Beljanski & Macheboeuf (1951) have found that penicillin inhibits the breakdown of guanosine by sensitive strains of Staph. aureus. Park & Johnson (1949) described the accumulation of labile phosphate compounds in Staph. aureus growing in the presence of penicillin, and Park (1952) identified three substances accumulating under these conditions; one of these is a derivative of uridine-5'-pyrophosphate and an N-acetylaminosugar, and the other two possess the same basic structure in combination with either L-alanine or a peptide containing L-lysine, Dglutamic acid and DL-alanine.

Techniques in tissue metabolism. 1. A mechanical chopper

Abstract: Richter, D. & Dawson, R. M. C. (1948). Amer. J. Phy8iol. 154, 73. Rosenberg, A. J., Buchel, L., Etling, N. & Levy, J. (1950). C.R. Acad. Sci., Pari8, 230, 480. Schmidt, C. F., Kety, S. S. & Pennes, H. H. (1945). Amer. J. Phy8iol. 143, 33. Schueler, F. W. & Gross, E. G. (1950). J. Pharmacol. 98,28. Stone, W. E. (1938). Biochem. J. 32, 1908. Swank, R. L. & Watson, C. W. (1949). J. Neurophy8iol. 12, 137. Warburg, 0. (1910). Hoppe-Seyl. Z. 68, 305. Webb, J. L. & Elliott, K. A. C. (1951). J. Pharmacol. 103, 24. Westfall, B. A. (1949). J. Pharmacol. 96, 193. Westfall, B. A. (1951). Amer. J. Phy8iol. 66, 219. Wikler, A. (1950). Pharmacol. Rev. 2, 435. Wilkins, D. S., Featherstone, R. M., Schwidde, J. T. & Brotman, M. (1950). J. Pharmacol. 98, 36. Zorn, C. M., Muntwyler, E. & Barlow, 0. W. (1939). J. Pharmacol. 66, 326.

The effect of calcium on the respiratory and phosphorylative activities of heart-muscle sarcosomes.

Abstract: 4. As a result of the findings, the suggestion is put forward that the levels of glutathione and ascorbic acid found in dietetic liver necrosis could be the result of changes occurring in a dead or dying liver left in the living body, and were not specific consequences of the dietetic lesion. Our thanks are due to Sir Harold Himsworth for his valuable advice and encouragement in this work. We are indebted to Miss S. Botha for her technical assistance. One of us (O. L.) was in receipt of a Research Grant from the Medical Research Council.

The differentiation of true and pseudo cholinesterase by organo-phosphorus compounds

Abstract: 1. Five preparations of testicular hyaluronidase, one of streptococcal and one of staphylococcal origin were compared by an accurate skin-diffuiion assay and by viscosimetric and turbidimetric methods. 2. With testicular preparations the results of the three methods agree well, provided that the potency is measured in terms ofa reference preparation of enzyme, and that the pH and ionic strength of the solvents are approximately physiological. It is desirable to use highly purified substrate, and to stabilize the enzymes with gelatin rather than gum acacia. 3. The activities of the two bacterial enzymes showed a close but not complete correlation between the three tests.

The determination of iron in blood plasma or serum.

Abstract: The author's original method 1 for the determination of iron in plasma or serum has been modified so as to eliminate filtration and give other advantages The new technique has been compared with others in current use