Molecular biology, Tris

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.

The first two volumes in the series New Comprehensive Biochemistry appeared in 1981. Volume 1 dealt with membrane structure and Volume 2 with membrane transport. The editors of the last volume (the present editor being one of them) tried to provide an overview of the state of the art of the research in that field. Most of the chapters dealt with kinetic approaches aiming to understand the mechanism of the various types of transport of ions and metabolites across biological membranes. Although these methods have not lost their significance, the development of molecular biological techniques and their application in this field has given to the area of membrane transport such a new dimension that the appearance of a volume in the series New Comprehensive Biochemistry devoted to molecular aspects of membrane proteins is warranted. 

Bioluminescence, the phenomenon of biological light emission, has fascinated mankind for many centuries. Scientists have been intrigued by it, and for many years have tried to answer simple questions like how and why certain animals and bacteria bioluminesce. This research has led to new insights in (molecular) biology and biochemistry. For example, in the 1960s, McCapra studied the chemical mechanisms of bioluminescence and devised a model for firefly luciferin the acridan esters (Fig. 1) [1-5],... 

We have tried throughout this book to use the enzyme name most commonly used by working biochemists and to point out cases in which an enzyme has more than one widely used name. For current information on enzyme nomenclature, refer to the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (www.chem.qmw.ac.uk/iubmb/nomenclature/). 

Alternatively, Sigma supplies phenol chloroform isoamyl alcohol 25 24 1 saturated with 10 mM Tris, pH8.0, 1 mM EDTA for use in molecular biology. 

Figure 7 Electronic absorption (Abs), magnetic circular dichroism (MCD), and circular dichroism (CD) spectra of mouse Cd7-MT-1 in 25 mM Tris/HCl, SOmMNaCl, pH 8.0. (Reproduced by permission of the American Society for Biochemistry Molecular Biology)...

It was a two-step publication. The main findings were published in two papers. One was a relatively small paper in the Journal of Molecular Biology [1984, 180, 385-398] on the arrangement of the chromophores in the reaction center. It was the most interesting information for all the people who were trying to understand the reaction centers. Then, about a year later we published a paper on the complete structure of the protein subunits that was in Nature [1985, 318, 618-624]. 

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