The Biochemical Society

Fig. 4.1.6 HPLC analysis of a sample of purified natural aequorin on a TSK DEAE-5PW column (0.75 x 7.5 cm) eluted with 10 mM MOPS, pH 7.1, containing 2mM EDTA and sodium acetate. The concentration of sodium acetate was increased linearly from 0.25 M to 0.34 M in 14 min after the injection of the sample. Full-scale 0.02 A. Flow rate 1 ml/min. Reproduced with permission, from Shimomura, 1986a. the Biochemical Society.

Fig. 4.1.8 Influence of various calcium chelators on the relationship between Ca2 " concentration and the luminescence intensity of aequorin, at 23-25°C (panel A) in low-ionic strength buffers (I < 0.005) and (panel B) with 150 mM KC1 added. Buffer solutions (3 ml) of various Ca2+ concentrations, pH 7.05, made with or without a calcium buffer was added to 2 pi of 10 pM aequorin solution containing 10 pM EDTA. The calcium buffer was composed of the free form of a chelator (1 or 2mM) and various concentrations of the Ca2+-chelator (1 1) complex to set the Ca2+ concentrations (the concentration of free chelator was constant at all Ca2+ concentrations). The curves shown are obtained with 1 mM MOPS (A), 1 mM gly-cylglycine ( + ), 1 mM citrate (o), 1 mM EDTA plus 2mM MOPS ( ), 1 mM EGTA plus 2 mM MOPS ( ), 2 mM NTA plus 2 mM MOPS (V), and 2 mM ADA plus 2 mM MOPS (A). In the chelator-free buffers, MOPS and glycylglycine, Ca2+ concentrations were set by the concentration of calcium acetate. Reproduced with permission, from Shimomura and Shimomura, 1984. the Biochemical Society.

Fig. 4.1.11 Influence of the concentration of apoaequorin on the yield of regenerated aequorin after 12 h at 4°C (solid line), and on the initial light intensity of the apoaequorin-catalyzed luminescence of coelenterazine (dashed line). The regenerated aequorin was measured with a 10 pi portion of a reaction mixture (0.5 ml) made with 10 mM Tris-HCl, pH 7.5, containing 1 mM EDTA, 5 mM 2-mercaptoethanol, 10 pi of methanolic 0.6 mM coelenterazine, and various amounts of apoaequorin. The luminescence activity of apoaequorin was measured in 2 ml of 10 mM Tris-HCl, pH 7.5, containing 0.5 M NaCl, 2 mM CaCb, 2 mM 2-mercaptoethanol, 10 pi of methanolic 0.2 mM coelenterazine, and various amounts of apoaequorin. Reproduced with permission, from Shimomura and Shimomura, 1981. the Biochemical Society.

Fig. 4.1.15 Comparison of the luminescence and fluorescence emission spectra of natural aequorin (left panel) and recombinant e-aequorin (right panel) the luminescence spectra of Ca2+ -triggered reaction (dark solid lines), the fluorescence emission spectra of the spent solution containing 2 mM Ca2+ (dashed lines), and the luminescence spectra of the spent solution after addition of coelenterazine (light solid lines). Reproduced with permission, from Shimomura, 1995d. the Biochemical Society.

Periodate Oxidation of Heparin and Related Compounds, A. B. Foster, R. Harrison, T. D. Inch, M. Stacey, and J. M. Webber, Biochem. /., 80 (1961) 12P-13P (Proceedings of the Biochemical Society 405th Meeting at Univ. of Birmingham, April 28-29, 1961). 

Fellow at St John s College and was awarded the Humphreys Research prize. At Cambridge, Nigel was a Research Fellow of the Royal Commission for the Exhibition of 1851 and Royal Society University Research Fellow. He was elected a Fellow of the Royal Society of Chemistry in 1997. Aged 36, Nigel is now Professor at Leicester University and Lister Institute Research Fellow. He is a recipient of the Colworth Medal of the Biochemical Society. His scientific interests include mechanistic and quantum enzymology his recreational interests include Victorian and College philately. 

Figure 1.2 Bonding in the diatomic oxygen molecule. Reproduced with permission from Halli-well and Gutteridge, 1984. the Biochemical Society.

Figure 10.3 (a) Proposed mechanism for induction of NFKB proteins (from Suzuki et al., 1994) (b) interaction with iron metabolism. Reproduced with permission from Cairo and Pietrangelo, 2000, the Biochemical Society. 

FIGURE 20-8 Linear representation of PKC isozymes. See text for details. Reproduced with permission from Tan, S. L. and Parker, R J. Biochemical Journal 376 545-552,2003 [23] The Biochemical Society. 

JondorfWR, Parke DV, Williams RT. 1957. The metabolism of [14C]hexachloroethane. In Proceedings of the Biochemical Society. 14P-15P. 

Smith, J. Prediction of putative reaction centres in Xenobiotics from metabolite using substructural fingerprinting. Transactions of the Biochemical Society. http //www.chemie.uni-erlangen.de/ dark/ smith/SPORCalc.html. 

Dunn, M. J. Gel Electrophoresis Proteins, Bios Scientific Publishers in Association with the Biochemical Society, Oxford, 1993. 

Archivist of the Biochemical Society, Dr. P.J. Fitzgerald, Professor Joel Mandelstam, and Dr. Michael Yudkin kindly read various drafts and made valuable suggestions. We are also particularly grateful to Dr. Michael Foster and Dr. Bruce Henning for their care in reading and correcting the manuscript. Any mistakes are ours, but they hopefully have been minimized thanks to the assistance of all of our friends in reviewing the material. 

Onodera played an important role on the editorial staffs of both the Agricultural Chemical Society and the Biochemical Society of Japan. In the Agricultural Chemical Society, he acted as Chairman of a branch of the Kansai district (west part of Japan) from 1967 to 1969. He was elected a member of the Science Council of Japan from 1968 to 1971. He was awarded the Suzuki prize by the Agricultural Chemical Society of Japan, the highest award of the Society, for his meritorious deeds in carbohydrate chemistry. But what he felt proudest of, and most honored about, was his appointment to the Editorial Board of Carbohydrate Research for 13 years (from 1966 to 1979). 

He devoted much energy to the 8th International Symposium on Carbohydrate Chemistry, held in the summer of 1975 in Kyoto. Japanese carbohydrate chemists belonged either to the Agricultural Chemical Society (to which Onodera belonged), the Biochemical Society, the Society of Pharmaceutical Science, or the Chemical Society of Japan. Consequently, the scientific papers, on carbohydrates, from Japan were published in various... 

Flypothetical interactions of a five-subsite enzyme with a maltotetraose substrate shown initially with a terminally radiolabeled (filled circles) nonreducing end. The vertical arrow indicates the glycosyl bond cleavage region the roman numerals indicate the subsites, and the 4 indicates the chain length. Only three binding interactions lead to hydrolysis IV,4 V,4 and Vl,4, and their different associated rate constants emphasize that the rates of hydrolysis need not be identical. From Allen and Thoma with permission of the Biochemical Society (London). 

Fig. 5. Scheme showing enzyme distribution in reverse micellar microenvironment. (Reproduced from [183] with permission of The Biochemical Society)... 

Kay, J. Weitzman, P.D.J. (eds) (1987) Krebs Citric Acid Cycle Haifa Century and Still Turning, Biochemical Society Symposium 54, The Biochemical Society, London. 

Sillen, L. G., Martell, A. E. Stability Constants of Metal-Ion Complexes, 2nd Ed. London The Biochemical Society 1964. 

Safety in Biological Laboratories (1977). Eds E. Hartree and V. Booth. London The Biochemical Society. 

Sargent, J.R. and Henderson, R.J. (1980). Lipid metabolism in marine animals. Transaction of the Biochemical Society 8,296-297. 

Simpson, D.J., I lover-1 Ianscn G., ChuaN.-H. and von Wettstein D. 1977. The use of gene mutants in barley to correlate thylakoid polypeptide composition with the structure of the photosynthetic membrane. In Photosynthesis 77. (Eds. D O. Hall, Coombs J., Goodwin T.W.) (The Biochemical Society, London), pp. 537-548. 

Professor Jones s participation in professional societies and affairs outside the University were as follows Rapporteur for the Royal Society of Canada (Chemical Section) in 1971, and Convenor in 1972 Member of the Advisory Committee to the Atlantic Regional Laboratories of the National Research Council, Halifax, Nova Scotia Member of the Board of Governors of the Ontario Research Foundation Member of the Board of Advisors for the British Commonwealth for Advances in Carbohydrate Chemistry and Biochemistry Member of the Editorial Advisory Board of Carbohydrate Research Chairman of the Fourth International Conference on Carbohydrate Chemistry, which was held in Kingston in 1967 and a Corresponding Member of the Nomenclature Committee of the Division of Carbohydrate Chemistry, American Chemical Society. Professor Jones was a member of The Chemical Society, the Biochemical Society, the Royal Institute of Chemistry (Associate), the Chemical Institute of Canada, the American Chemical Society, and the New York Academy of Sciences. 

I am indebted to the American Chemical Society, the Biochemical Society, the Chemical Society, the Faraday Society, the Royal Society, the Zeitschrift fur physikalische Chemie, and the proprietors of Reviews of Modem Physics, for permission to reproduce various diagrams not found in the first edition. 

Admission to the Royal Institute of Chemistry resulted from the accidental admission of a woman to the Institute s examinations in 1892, and the Biochemical Society, by vote of the existing members, first accepted women in 1913. The major holdout was the Chemical Society with its Forty Years War, as Joan Mason, historian of chemistry, called it (see below) not until 1920 were women admitted to the Chemical Society. But the last of all was the Royal Society, which did not elect its first women Fellows until 1948, both of whom were chemists. 

Ida Smedley25 was a key individual in the early advancement of women in chemistry. As we have seen above, she was one of the first women members of the Biochemical Society but of more importance, as we will see shortly, she was one of the two women (Martha Whiteley — see Chap. 3 — being the other) who fought for decades for the admission of women to the Chemical Society. 

By 1913, Wheldale s fame was such that she was one of the first three women (the other two being Ida Smedley and Harriette Chick see Chap. 2) to be elected to the Biochemical Club,43 the forerunner of the Biochemical Society. She was also awarded a Prize Fellowship in 1915 by the British Federation of University Women for her scientific research. 

Goodwin, T. W. (1987). History of the Biochemical Society 1911-1986. Biochemical Society, London. 

Coward was professionally active, being a member of the Vitamin Committee of the British Pharmacopoeia Commission from 1933 to 1953 and a member of the Committee of the Biochemical Society from 1932 until 1936 and in 1937, she was elected as an honorary member of the Pharmaceutical Society. Her advice was sought by committees of the League of Nations and the World Health Organisation. She retired in 1950, but continued to be active, as her obituarist, G. S. Cox, recalled ... 

Figure 4.3. Treatment with single stranded RNA targeted against TRPCl inhibits maitotoxin-induced [Ca +]i increment in H4-IIE hepatoma cells. (Reproduced with permission from Chen and Barritt 2003, the Biochemical Society).

FIGURE 5. The absorption spectrum of MDH lacking calcium (broken line), isolated from mxaA mutant, and the effect of incorporation of calcium into the enzyme (solid line). Reproduced with permission from Goodwin et al. (1996), Biochemical Journal, 319, 839n842). the Biochemical Society. 

FIGURE 6. The reduction of oxidised Ba-MDH by endogenous substrate. MDH lacking any metal ion in its active site was produced from the mxaA mutant it was incubated with Ba + to produce Ba-MDH which was then oxidised with a small excess of Wursteris Blue which was then removed by rapid gel filtration and spectra recorded. Reproduced with permission from Goodwin and Anthony (1996), Biochemical Journal, 318, 673n679). the Biochemical Society. 

Figure 5 Fourier filtered EXAFS data (R = 4.6-5.S A)ofZii7-MT from rabbit liver and a theoretical simulation with two Zn-Zn separations at 4.8 A and 5 A. (Reproduced with permission from Ref. 34. the Biochemical Society)...

Figure 11 Representative EPR powder spectra of different classes of common FeS clnsters. All spectra represent clusters in the paramagnetic 5 = 1/2 state. (Reproduced with pennission from Cammack, Path and Fernandez. 1985 The Biochemical Society)...

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