For biochemistry

The Chemical Abstracts (CA) File is the main abstracting and indexing service for biochemistry, chemistry, and chemical engineering. 

Biophys 111 8 1965.] For biochemistry see Blakley Biochemistry of Folic Acid and Related Pteridines North Holland Publ Co, Amsterdam 1969 ]... 

American Society for Biochemistry and Moiecuiar Bioiogy (ASBMB)... 

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.

Thermodynamic data for Biochemistry and Biotechnology, Hans-Jurgen Hinz, Ed. (Springer-Verlag, Berlin, 1986) p. 45. 

N. V. Bovin and H.-J. Gabius, Polymer immobilized carbohydrate ligands versatile chemical tools for biochemistry and medical science, Chem. Soc. Rev., 24 (1995) 413—421. 

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. 

The AE blend Brij 35 with the general formula CnH2n+i 0(CH2CH20)mH was analysed by MALDI MS prior to use for biochemistry research. Separation results of thin-layer (TLC) and RP-LC of these surfactants were compared [30]. Brij 35, as a mixture of Ci2 and C14 homologues (to = 15-39), was detected qualitatively as [M + Na]+ and [M + K]+ ions and quantitatively after TLC and RP-LC separation. 

Department of Protein Crystallography Max-Planck-Institute for Biochemistry Am Klopferspitz 18 a 82152 Martinsried Germany... 

Department of Structural Biology Max-Planck-lnstitute for Biochemistry 82152 Martinsried Germany Kevin L. Lorick NCI at Frederick Building 560, Room 22-103 1050 Boyles Street Frederick, MD 21702 USA... 

N. BORGESE, CNR Center for Cytopharmacology, University of Milan, Milan, Italy D. DASGUPTA, Saha Institute of Nuclear Physics, Calcutta, India H. ENGELHARDT, Max-Planck-Institute for Biochemistry, Martinsried, Germany A.-H. ET EMADI, University of Paris VI, Paris, France... 

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.

Manuals m Biomedical Research — VoL 3 A MANUAL FOR BIOCHEMISTRY PROTOCOLS... 

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...

Figure 12.6 Effector mechanism activation of adenyi cyclase via a G-protein. The activation of adenyi cyclase, which resides on the cytosolic side of the cell membrane, is mediated through the membrane-bound G-protein system (see below for biochemistry and role of the G-protein). An example is adrenaline binding to the p-receptor.

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.

Current address Laboratory for Biochemistry, State University Ghent, K L. Ledeganckstraat 35, B-9000 Ghent, Belgium... 

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.

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