Showing papers in "Biochemical Journal in 1958"

Turnover of protein in growing and non-growing populations of Escherichia coli.

Abstract: Britten, R. J., Roberts, R. B. & French, E. F. (1955). Proc. nat. Acad. Sci., Wash., 41, 863. Cohen, G. N. & Rickenberg, H. V. (1955). C.R. Acad. Sci., Paris, 240, 2086. Cohen, G. N. & Rickenberg, H. V. (1956). Ann. Inst. Pasteur, 91, 693. Dagley, S. & Johnson, A. R. (1956). Biochim. biophys. Acta, 21, 270. Gale, E. F. & Epps, H. M. R. (1944). Biochem. J. 38, 232. Halvorson, H., Fry, W. & Schwemmin, D. (1955). J. gen. Physiol. 38, 549. Hirsch, M. L. & Cohen, G. N. (1953). Biochem. J. 53, 25. Kay, R. E., Harris, D. C. & Entenman, C. (1956). Arch. Biochem. Biophys. 63, 14. Mandeistam, J. (1954). J. gen. Microbiol. 11, 426. Mandelstam, J. (1955). Ab8tr. 3rd Int. Congr. Biochem., Bru8set8, p. 98. Mandelstam, J. (1956a). Biochem. J. 64, 55P. Mandelstam, J. (1956b). Biochim. biophy8. Acta, 22, 313. Mandelstam, J. (1957). Nature, Lond., 179, 1179. Markovitz, A. & Klein, H. P. (1955). J. Bact. 70, 649. Piper, E. A. & Arnstein, H. R. V. (1956). Biochem. J. 64, 57P. Polson, A. (1948). Biochim. biophys. Acta, 2, 575. Proom, H. & Woiwod, A. J. (1949). J. gen. Microbiol. 3, 319. Rickenberg, H. V., Cohen, G. N., Buttin, G. & Monod, J. (1956). Ann. In8t. Pasteur, 91, 829. Taylor, E. S. (1947). J. gen. Microbiol. 1, 86. Work, E. (1949). Biochim. biophys. Acta, 3, 400.

A study of the inhibition of catalase by 3-amino-1:2:4:-triazole.

Abstract: Olcott, H. S. & Fraenkel-Conrat, H. (1947). Chem. Rev. 41, 151. Pouradier, J., Venet, H. M. & Trigny, L. (1955). Proc. 27th Congr. Int. Chim. Ind., Brussels, 3, 709. Reitz, H. C., Ferrel, R. E., Fraenkel-Conrat, H. & Olcott, H. S. (1946). J. Amer. chem. Soc. 68, 1024. Saunders, P. R., Stainsby, G. & Ward, A. G. (1954). J. Polym. Sci. 12, 325. Saunders, P. R. & Ward, A. G. (1953). Proceedings of the 2nd International Congress on Rheology, p. 284. London: Butterworths Scientific Publications. Saunders, P. R. & Ward, A. G. (1955). Nature, Loud., 176, 26. Stainsby, G. (1956). Nature, Lond., 177, 745. Synge, R. L. M. (1939). Biochem. J. 33, 1913. Tedder, J. M. (1955). Chem. Rev. 55, 787. Udenfriend, S. & Cooper, J. R. (1952). J. biol. Chem. 196, 227. Ward, A. G. (1953). Nature, Lond., 171, 1100. Ward, A. G. (1955). Nature, Lond., 175, 289. Wolfrom, M. L., Konigsberg, M. & Soltsberg, S. (1936). J. Amer. chem. Soc. 58, 490.

The occurrence and distribution of thymine and three methylated-adenine bases in ribonucleic acids from several sources

Abstract: It has been known for several years that deoxyribonucleic acid may normally contain 5-methylcytosine (Wyatt, 1951), 5-hydroxymethylcytosine (Wyatt & Cohen, 1953), and 6-methylaminopurine (Dunn & Smith, 1955, 1958a) in addition to adenine, guanine, cytosine and thymine. The first evidence of such additional bases naturally present in ribonucleic acid is the recent isolation of an unidentified nucleotide from the ribonucleic acid of yeast (Cohn, 1957; Davis & Allen, 1957). During studies on the incorporation of unnatural bases, Dr J. D. Smith and one of us (D. B. D.) each noted that digests of ribonucleic acid from E8cherichia coli contained a compound with spectral and chromatographic characteristics which suggested that it was the riboside of thymine (J. D. Smith, unpublished work; Dunn, 1957). The present work has not only confirmed this finding but has indicated that three methylated adenine bases, 2-methyladenine, 6methylaminopurine and 6-dinethylaminopurine, as well as thymine, are naturally present in small amounts in ribonucleic acid from a variety of sources. None of these compounds has been described previously as a component of ribonucleic acid, but all four are known to occur naturally as nucleosides or nucleotides, since thymine and 6methylaminopurine occur in deoxyribonucleic acid (Kossel & Neumann, 1893; Dunn & Smith, 1958a), 2-methyladenine in the vitamin B12-like Factor A extracted from E. coli and other sources (Dion, Calkins & Pfiffner, 1954; Brown, Cain, Gant, Parker & Smith, 1955) and 6-dimethylaminopurine in puromycin formed by the actinomycete Streptomyces alboniger (Waller, Fryth, Hutchings & Williams, 1953). The presence of 6-methylaminopurine in ribonucleic acid from yeast has also been reported by Adler, Weissmann & Gutman (1958). This paper describes the isolation of the ribosides and ribotides of these compounds from several ribonucleic acids and their identification by chromatographic, electrophoretic and spectroscopic methods. Preliminary results of this work have been reported (Littlefield & Dunn, 1958a, b).

The occurrence of 6-methylaminopurine in deoxyribonucleic acids.

Abstract: While investigating the effects of structural analogues of thymine on the thymine-requiring strain of E&cherichia coli 15 T we noticed the presence in the bacterial deoxyribonucleic acid of a new base which we have identified as 6-methylaminopurine. Although 6-methylaminopurine is usually present in small amounts (2% of the adenine) in the deoxyribonucleic acid of E. coli 15 Tits relative proportion increases considerably during growth of the bacteria in thymine-deficient conditions, obtained either by maintaining the thymine concentration in the medium at a low level, or by the addition of thymine antagonists such as 5-aminouracil or 2-thiothymine. Examination of a number of deoxyribonucleic acids has shown that 6-methylaminopurine also occurs in small proportions as a constituent of deoxyribonucleic acid from several bacteria and bacterial viruses. This paper describes the identification of 6-methylaminopurine, its deoxyribonucleoside and deoxyribonucleotide from deoxyribonucleic acid of E. coli 15 T, and the occurrence of the base in other deoxyribonucleic acids. Brief accounts of this work have appeared previously (Dunn & Smith, 1955a, b).

The production of secondary potassium depletion, sodium retention, nephrocalcinosis and hypercalcaemia by magnesium deficiency.

Abstract: Studies of dietary magnesium depletion in the rat have been made by Kruse, Orent & McCollum (1932), Watchorn & McCance (1937) and Tufts & Greenberg (1938). These workers reported an early stage of vasodilatation and hyperexcitability followed by a chronic stage of cachexia. Little or no change was found in the magnesium content of the tissues other than bone, teeth and serum (Watchorn & McCance, 1937), although Tufts & Greenberg (1938) reported minor changes in muscle and brain. The failure of magnesium-deficient diets to produce changes of magnesium content in the soft tissues contrasts with the marked decreases in muscle potassium produced by potassium deficiency (Heppel, 1939). For this reason it was considered that a fuller investigation of magnesium deficiency was necessary. This has been undertaken by using specific flame-spectrophotometric techniques.

Regulation of glucose uptake by muscle. 2. The effects of insulin, anaerobiosis and cell poisons on the penetration of isolated rat diaphragm by sugars.

Abstract: The utilization of glucose by muscle is thought to be limited by the rate at which glucose enters the muscle cell and insulin is believed to stimulate glucose uptake by speeding its entry (Levine & Goldstein, 1955; Park, Bornstein & Post, 1955; Park & Johnson, 1955). We have shown that the uptake of glucose by isolated rat diaphragm incubated in a bicarbonate-buffered medium is increased by anoxia and by substances which inhibit oxidative phosphorylation, as well as by insulin (Randle & Smith, 1957, 1958). These observations led us to suggest that the entry of sugars such as glucose into the muscle cell is restrained under basal conditions by a process dependent upon a supply of energy-rich phosphate. We have now attempted to obtain more direct evidence in support of this suggestion by studying the effects of insulin, anaerobiosis and substances which inhibit oxidative phosphorylation on the accumulation of glucose and xylose in isolated diaphragm. We will express the amount of glucose or xylose accumulating in diaphragm as a space, the glucose or xylose space being that fraction of the volume of the tissue which appears to contain fluid of the same specific gravity and glucose or xylose content as the incubation medium. Interpretation of these results in terms of the distribution of sugar between extracellular and intracellular water in-

The nature of the thyroid auto-antibodies present in patients with Hashimoto's thyroiditis (lymphadenoid goitre).

Abstract: We are indebted to Dr Rita H. Cornforth of the National Institute for Medical Research for the synthesis of [2-14C]mevalonic acid; to Professor A. Wormall, F.R.S., for a gift ofsqualene and to Horlicks Ltd. for a supply of ,B-mercaptoethylamine (Becaptan). The spectroscopic examination of the microsomes were done by Dr F. A. Holton. It is a pleasure to acknowledge the skilled technical assistance of Mr K. Clifford and Mr T. Flynn. A grant from the Eli illy Foundation to the Medical Research Council for the purchase of our Spinco Model L centrifuge is also gratefully acknowledged.

Biochemical studies of toxic agents. 11. The occurrence of premercapturic acids.

Abstract: Baumann & Preusse (1879) and Jaff6 (1879) showed that the mercapturic acids which they isolated from the urine of dogs dosed with bromobenzene or chlorobenzene were formed by the decomposition of acid-labile compounds in the urine, and they believed that these precursors were derivatives of glucuronic acid. This work has recently been revised and extended as a result of the findings of Boyland, Sims & Solomon (1957) and Knight & Young (1957). From the urine of rabbits dosed with naphthalene, Boyland et al. (1957) and Boyland & Sims (1958) isolated a compound which on acidification yielded 1and 2naphthol as well as 1-naphthylmercapturic acid, and they suggested that the compound is N-acetylS-(2-hydroxy1:2-dihydro 1 naphthyl)-Lcysteine. They also stated that anthracene and bromobenzene appear to give similar metabolites. The present paper contains an account of chromatographic studies which have shown that the administration of benzene, naphthalene, anthracene, fluorobenzene, chlorobenzene, bromobenzene and iodobenzene to rabbits or rats is followed by the excretion of acid-labile precursors of the corresponding mercapturic acids. In a preliminary account of this work (Knight & Young, 1957) the name 'premercapturic acid' was proposed for such precursors. The radiochromatographic examination of urine containing 35S-labelled 1-naphthylpremercapturic acid or p-bromophenylpremercapturic acid has indicated that acid decomposition of a premercapturic acid can lead to the formation of another sulphur-containing compound in addition to the mercapturic acid. Furthermore, by means of isotope-dilution techniques it has been possible to show that the amount of l-naphthylmercapturic acid which can be liberated by mineral acid in the urine of rats dosed with naphthalene depends on the pH at which the 1-naphthylpremercapturic acid breaks down. Not all the mercapturic acids isolated from urine are derived from the decomposition of premercapturic acids, for chromatographic studies and tracer-isotope experiments have led to the conclusion that the urine of rats dosed with benzyl chloride does not contain an acid-labile precursor of benzylmercapturic acid. * Part 10: Marsden & Young (1958). CHROMATOGRAPHIC STUDIES

Formation of specific antibodies and γ-globulin in vitro. A study of the synthetic ability of various tissues from rabbits immunized by different methods

Abstract: Although there is abundant evidence that specific antibodies are formed in lymphoid tissues (e.g. spleen and lymph nodes) of immunized animals, relatively little is known about the extent to which different tissues contribute to overall synthesis of specific antibody or of other y-globulin in the whole animal. [14C]Glycine has been shown to be incorporated into antibody by slices of spleen and liver taken from animals immunized intravenously (Ranney & London, 1951; Keston & Dreyfus, 1951), and by granulomatous tissue developed at the site of administration of antigen in an adjuvant mixture (Askonas & Humphrey, 1955). When the relative rates of incorporation of labelled amino acid into antibody by tissue slices taken from different organs of the guinea pig were compared with the populations of antibody-containing cells in those organs, Askonas & White (1956) found a generally good correlation between the two measurements. There is therefore some justification for considering that the ability of tissues to incorporate amino acids into specific antibody or other y-globulin in vitro, under suitable experimental conditions, is a measure of the relative ability of the tissues to synthesize these proteins. Because of its simplicity we have used this method to study antibody synthesis by different tissues in rabbits immunized with one or more antigens and by different routes. Our results show that the pattern of antibody synthesis varies widely under different conditions, but that it is always accompanied by increased synthesis of other y-globulin. The reasons for this and the mechanism of formation of these proteins by the tissue slices are discussed.

Extraction of proteins other than myosin from the isolated rabbit myofibril.

Abstract: Barton, G. M., Evans, R. S. & Gardner, J. A. F. (1952). Nature, Loud., 170, 249. Bernstein, S. & McGilvery, R. W. (1952a). J. biol. Chem. 198, 195. Bernstein, S. & MeGilvery, R. W. (1952b). J. biol. Chem. 199, 745. Bush, I. E. & Willoughby, M. (1957). Biochem. J. 67,689. De Meio, R. H. & Lewycka, C. (1955). Endocrinology, 56, 489. De Meio, R. H. & Tkacz, L. (1952). J. biol. Chem. 195, 175. De Meio, R. H. & Wizerkaniuk, M. (1956). Biochim. biophy8. Acta, 20, 428. De Meio, R. H., Wizerkaniuk, M. & Fabiani, E. (1953). J. biol. Chem. 203, 257. De Meio, R. H., Wizerkaniuk, M. & Schreibman, I. (1954). Fed. Proc. 13, 198. De Meio, R. H., Wizerkaniuk, M. & Sohreibman, I. (1955). J. biol. Chem. 213, 439. Gregory, J. D. & Nose, Y. (1957). Fed. Proc. 16, 189. Markham, R. & Smith, J. D. (1952). Biochem. J. 52, 552. Pearlman, W. H. & De Meio, R. H. (1949). J. biol. Chem. 179, 1141. Pincus, G. & Pearlman, W. H. (1941). Endocrinology, 29, 413. Roy, A. B. (1956). Biochem. J. 63, 294. Segal, H. L. (1955). J. biol. Chem. 213,161. Stevenson, M. F. & Marrian, G. F. (1947). Biochem. J. 41, 507.