American Society for Biochemistry and Molecular Biology

American Petrofina, See TotalFinaElf (France), 216 American Petroleum Institute (API), 268 American Plastics Council (APC), 268 American Polyolefin Association, Inc. (APA), 268 American Samoa Environmental Protection Agency, 289 American Society for Biochemistry and Molecular Biology (ASBMB), 268... 

Fig. 10.4.1 Light emission profile of the luminescence reaction of the acorn worm Balanoglossus biminiensi, when H2O2 is injected into a mixture of the luciferin and luciferase. From Dure and Cormier, 1961, with permission from the American Society for Biochemistry and Molecular Biology.

Fig. 10.4.2 The effects of temperature (left panel) and pH (right panel) on the peak intensities of the Balanoglossus luminescence reaction. In the measurements of the temperature effect, 0.5 ml of 0.176 mM H2O2 was injected into a mixture of 1.2 ml of 0.5 M Tris buffer (pH 8.2), 0.3 ml of luciferase, and 1 ml of luciferin, at various temperatures. For the pH effect, the Tris buffer (pH 8.2) was replaced with the Tris buffers and phosphate buffers that have various pH values, and the measurements were made at room temperature. From Dure and Cormier, 1963, with permission from the American Society for Biochemistry and Molecular Biology.

Prescott, M. P. (ed.) A thematic series on phospholipases. Journal of Biological Chemistry 1997 Minireview Compendium. Bethesda, MD American Society for Biochemistry and Molecular Biology, 1997. 

Figure 11.3. The active site of Cab. Reprinted with permission from Strop et al. (2001), copyright 2001 American Society for Biochemistry and Molecular Biology.

Fig. 12.4 Functional coupling of the Gly389 and Arg389 receptors to adenylyl cyclase. (Reproduced from ref. 26 with permission of the American Society for Biochemistry and Molecular Biology.) Shown are the results from studies with clonal lines expressing each receptor at matched levels and the data presented as absolute activities (A) and normaUzed to the stimulation by forskolin (B). The results of similar studies with two other clonal lines are shown in C and D. The Arg389 demonstrated small increases in basal activities and marked increases in agonist-stimulated activities compared with the Gly389 receptor. Shown are the mean results from four independent experiments carried out with each line. Absent error bars denote that standard errors were smaller than the plotting symbol...

Fig. 10. A. Acetic acid-urea-triton-X-100 polyacrylamide gel electrophoresis [15] of the histones used to reconstitute 208-12 nucleosome arrays consisting of recombinant H2A.Z (lane 2) or recombinant H2A.1 (lane 3). Lanes 1 and 4 respectively are chicken erythrocyte and calf thymus histones used as markers [42]. B. Ionic strength (NaCl concentration) dependence of the average sedimentation coelRcient (s2o,w) of reconstituted 208-12 nucleosome arrays containing either H2A.1 (O) or H2A.Z ( ) [42]. The dotted line represents the behavior of a 208-12 complex reconstituted with chicken erythrocyte histones [406]. [Reproduced from Abbott D.W. et al. (2001) I. Biol. Chem. 276, 41945-41949, with permission from The American Society for Biochemistry and Molecular Biology.]...

B. Effect of the ionic strength on hyperacetylated 208-12 nucleosome arrays as visualized by electron microscopy. The numbers to the left indicate the milimolar NaCl concentration [369]. [Reproduced from Garcia-Ramirez M. et al. (1995) J. Biol. Chem. 270, 17923-17928, with permission from The American Society for Biochemistry and Molecular Biology.]... 

Figure 5. Summary of amino acid sequence homology between different xylose isomerases. The percent of homology was calculated by using the University of Wisconsin Genetics Computer Group, version 5, program (Devereux, L, Haeberli, P., and Smithies, O. Nucleic Acids Res. 12, 387-395, 1984). Reprinted with permission from ref. 22. Copyright 1990 American Society for Biochemistry and Molecular Biology.

Figure 1. Top Turbidity, measured at 350 nm, as a function of microtubule polymer mass concentration (expressed as mg/mL polymerized tubulin). Tubulin solutions of varying concentrations were polymerized until they reached stable plateau values in a Cary 118C spectrophotometer. Each sample was then transferred to an ultracentrifuge tube, and microtubules were pelleted, separated from the unpolymerized tubulin in the supernatant fraction, and then resuspended for protein concentration determination. The corresponding turbidity and polymer mass concentrations are plotted here. Bottom Time-course of tubulin polymerization assayed by turbidity.Repro-duced from MacNeal and Purich with permission from the American Society for Biochemistry and Molecular Biology.

Interleukin 1-induced formation of iron-nitrosyl complexes by rat islets. Rat islets were incubated fot 18 hr in the presence or absence of 5 U/ml lL-1, 0.5 mM NMMA, or lL-1 and NMMA. The islets were isolated and the fotmation of nitric oxide was examined by EPR spectroscopy as described previously (Corbett et al., 1991a). IL-1 induces the formation of a g = 2.04 featute that is characteristic of the fotmation of iton-nittosyl complexes, and NMMA ptevents the formation of this axial g = 2.04 iton-nittosyl feature. Also shown is the simultaneous formation of nitrite by the same islets used for EPR spectroscopy. Repnxluced with permission from ]. Biol. Chem. (Corbett et al., 1991a), from the American Society for Biochemistry and Molecular Biology. 

American Society for Biochemistry and Molecular Biology (ASBMB)... 

All reprinted parts of this paper (cited in Footnote 1) appear with the permission of Professor Leonard J. Banaszak and the American Society for Biochemistry and Molecular Biology, Inc., publisher of Journal cf Biological Chemistry. 

Fig. 5 Cationic lipids DORIE, DORIE-HP, DORIE-HB, DORIE-HPe, containing increasing numbers of methylene groups between the hydroxyl and amine moieties, and DOTMA, which lacks hydroxyl group, formulated with 50 mol% DOPE, and assayed for transfection (reproduced from [35] copyright by the American Society for Biochemistry and Molecular Biology)...

Figure 1.10 UV-VIS absorbance of the H404A mutant of VCPO and the effect of H2O2 at pH 8.3. (a) Spectrum a 200 /xM apo-H404A spectrum b mixture of holo- and apo-enzyme after addition of 200 fxM vanadate spectrum c the effect of addition of 200 (xM H2 O2. (b) Spectrum a titration of 200 fxM apo-H404A with 0-800 /xM vanadate the line shown is a fit to the data points for a simple dissociation equilibrium spectrum b absorbance of 0-200 fxM free vanadate. Source Renirie, R., Hemrika, W. and Wever, R. (2000). Journal of Biological Chemistry, 275, 11650-11657. Reprinted with permission from The American Society for Biochemistry and Molecular Biology.

Figure 8.5 PolyP accumulation, and polyphosphate kinase (PPK) and exopolyphosphatase (PPX) activities, under stringent conditions. E. coli MG1655 was grown on a MOPS medium containing 0.4 mM P . At A540 near 0.2, serine hydroxamate (SHX) was added (0.5 mg mO1) for induction of amino acid starvation and accumulation of (p)ppGpp. Symbols represent with ( ) and without (<0>) serine hydroxamate units of PPK and PPX in (b) are 1 nmol P muT1 (Kuroda et al., 1997). Reproduced with permission from Kuroda, A., Murphy, H., Cashel, M. and Kornberg, A., J. Biol. Chem., 272(34), 21240-21243 (1997). Copyright (1997) American Society for Biochemistry and Molecular Biology.

Scheme 4 Proposed catalytic mechanism of PHM and D/3M showing the reactive ternary complex. Proposed structure of the intermediate formed after reaction of Cub(H)-02 with substrate to form a substrate-derived free radical and Cub(11)-OOH. This illustrates a possible pathway for electron transfer from QiaCI) to Cub(H)-OOH throngh the solvent-filled cleft and the changes in copper ligation that accompany oxidation. With the exception of reactive intermediates, the water molecules complexed to the copper sites have been omitted. (Ref 27, Reproduced by permission of American Society for Biochemistry and Molecular Biology)...

Figure 5 Proposed catalytic cycle for NO reductase from Pseudomonas aeruginosa (a) and EPR spectra of freeze-quenched samples (b). A The catal)dic nonheme iron Fen, the high-spin heme b, the low-spin heme b, and heme c are indicated from right to left in each state. B Panels A and B show the spectra recorded at 11 and 35 K after atmealing, respectively. Traces a-f show the X-band EPR spectra for the samples quenched at 0.5 ms after mixing the fully reduced NOR with NO buffer and atmealing at 193 K for 120min (trace a), 223 K for 5 min (trace b), 243 K for 5 min (trace c), 263 K for 10 min (trace d), 263 K for 30 min (trace e), and 263 K for 90 min (trace f). The g-values are indicated for the various species. (Reproduced from Kumita, Matsuura, Hino, Takahashi, Hori, Fukumori, Morishima and Shiro by permission of American Society for Biochemistry and Molecular Biology)...

Journal of Biological Chemistry [J. Biol. Chem.] (1905-). Free online full-text archive. Publisher The American Society for Biochemistry and Molecular Biology. 

Figure 11.10. Two-dimensional separation of E. coli protein mixture, using IEF with carrier ampholytes, pH range 3-10, in the first (horizontal) direction, and SDS-PAGE was mn from top to bottom in the second dimension on a 9-14% polyacrylamide gradient running gel cast with 0.1% SDS.12 [Reprinted, with permission, from P. H. O Farrell, The Journal of Biological Chemistry 250 (No. 10 May 25), 1975, 4007 4021. High Resolution Two-Dimensional Electrophoresis of Proteins . Copyright 1975 by the American Society for Biochemistry and Molecular Biology, Inc.]...

A control protein, CAT, is used to show data reliability. [Reprinted, with permission, from V. J. Hindson, P. C. E. Moody, A. J. Rowe, and W. V. Shaw, The Journal of Biological Chemistry 275, No. 1, 2000, 461-466. Serine Acetyltransferase from Escherichia coli Is a Dimer of Trimers . Copyright 2000 by The American Society for Biochemistry and Molecular Biology, Inc.]... 

Figure 8 Region of the anomeric diagonal of the 300-ms 2D NOESY spectrum of the 35-nt extended dimer stem-loop SL1 RNA from HIV-1. Peaks labeled only with numbers denote residue numbers for H1 -H1 cross-peaks cross-strand crosspeaks are labeled in italics. Reproduced with permission from N. B. Ulyanov A. Mujeeb Z. Du M. Tonelli T. G. Parslow T. L. James, J. Biol. Chem. 2006,281,16168-16177. Copyright 2006 American Society for Biochemistry and Molecular Biology.

Figure 4-14. Catalytic voltammetry of nitrite reductase is critically dependent on the identity and concentration of the substrate at pH 7. (A) In 1 pM nitrite, reduction of the enzyme successively, turns on, but then attenuates activity. (B) Overlaid derivatives emphasise changes in the waveshape as the nitrite concentration is increased from 1.7 to 265 pM. At higher nitrite concentrations, activity increases upon application of a more negative potential, and this is reflected by the two positive features in the derivative plot. (C) At 1 mM hydroxylamine, reduction of the enzyme does not attenuate the rate of catalysis. (D) Overlaid derivatives show that as the hydroxylamine concentration is raised from 1.1 to 347 mM the waveshape develops two positive features similar to the waveshapes displayed at high rates of nitrite reduction. Reproduced from ref. 70 with permission of the American Society for Biochemistry and Molecular Biology.

Fig. 14.2 Conventional representation of the transport protein of maltodextrin. The P-folds are represented by arrows. The sequence order of the j8-folds in the polypeptide chain is indicated by letters and those of the helices by Roman numerals. The site of the maltose, in the centre, is indicated by two large black dots connected by a vertical bar (Spurlino et al. 1991) (reproduced with kind permission from the American Society for Biochemistry and Molecular Biology and the authors).

Molecular and Cellular Proteomics. Bethesda, MD American Society for Biochemistry and Molecular Biology. Monthly. ISSN 1535-9476. Scope includes structural and functional properties of proteins and their expression, developmental time courses of the organism, how the presence or absence of proteins affects biological responses and how the interaction of proteins with germane cellular partners allows them to function, and advances in methodology, array technologies, changes in expression of the proteins, calculations and/or predictions, and aspects of bioinformatics that address needs in proteomics. 

Perry Allen Frey was born in Plain City, OH, USA on 14 November 1935. After graduating from the local high school, he served 2 years in the US Army and then studied chemistry at The Ohio State University, graduating in 1959 with a BS degree in chemistry. He worked as a chemist for the US Public Health Service from 1960 to 1964. He was a predoctoral fellow of the National Institutes of Health (NIH) from 1964 to 1967 and received the Ph.D. degree in biochemistry from Brandeis University in 1968. He was a postdoctoral fellow of the NIH at Harvard University in 1968. In 1969, he became an assistant professor of chemistry at The Ohio State University where he rose to professor of chemistry. In 1981, he moved to the University of Wisconsin-Madison as professor of biochemistry, and was the Robert H. Abeles Professor from 1993 to 2008 and is currently Emeritus Professor. He is a member of the American Association for the Advancement of Science (AAAS), the American Chemical Society, the American Society for Biochemistry and Molecular Biology, and the Protein Society. He is a member of the National Academy of Sciences and a Fellow of the American Academy of Arts and Sciences and a Fellow of the AAAS. 

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