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Biochemistry: The

Data from CRC Handbook of Biochemistry, The Chemical Rubber Co., 1968. [Pg.47]

Cells make use of many different types of membranes. All cells have a cytoplasmic membrane, or plasma membrane, that functions (in part) to separate the cytoplasm from the surroundings. In the early days of biochemistry, the plasma membrane was not accorded many functions other than this one of partition. We now know that the plasma membrane is also responsible for (1) the exclusion of certain toxic ions and molecules from the cell, (2) the accumulation of cell nutrients, and (3) energy transduction. It functions in (4) cell locomotion, (5) reproduction, (6) signal transduction processes, and (7) interactions with molecules or other cells in the vicinity. [Pg.260]

Advances in biochemical knowledge have illuminated many areas of medicine. Conversely, the study of diseases has often revealed previously unsuspected aspects of biochemistry. The determination of the sequence of the human genome, nearly complete, will have a great impact on all areas of biology, including biochemistry, bioinformatics, and biotechnology. [Pg.4]

The fundamental role of blood in the maintenance of homeostasis and the ease with which blood can be obtained have meant that the study of its constituents has been of central importance in the development of biochemistry and clinical biochemistry. The basic properties of a number of plasma proteins, including the immunoglobulins (antibodies), are described in this chapter. Changes in the amounts of various plasma proteins and immunoglobulins occur in many diseases and can be monitored by electrophoresis or other suitable procedures. As indicated in an earlier chapter, alterations of the activities of certain enzymes found in plasma are of diagnostic use in a number of pathologic conditions. [Pg.580]

The aim of this review was to summarize those aspects of fluorescence spectroscopy that may have value for solving problems in food science and technology. The techniques described, which are mainly based on front-face fluorescence spectroscopy coupled with multidimensional statistical methods, have been illustrated by examples taken from the literature and the work done in our laboratory. Although fluorescence spectroscopy is a technique whose theory and methodology have been extensively exploited for studies of both chemistry and biochemistry, the utility of fluorescence spectroscopy for molecular studies has not yet been fully recognized in food science. Fluorescence spectroscopy has the same potential to address molecular problems in food science as in the biochemical science field, because the scientific questions that need to be answered are closely related. We hope that this coverage will introduce a novel class of techniques in the emulsion and gel fields. [Pg.287]

A. L. Lehninger, Biochemistry. The Molecular Basis of Cell Structure and Function, Worth, New York, 1972. [Pg.760]

Marc Van Regenmortel. Yes, I would agree with one of the earlier speakers who put the emphasis on analysis. As I mentioned, analysis is a matter of dissection and in that sense you have to be reductionist. You can t dissect without being a reductionist but the only thing you are achieving is a description of the constituent parts. Whether you like the word level does not matter. Physiology will never be transformed into biochemistry. The same phenomenon can of course be described at different levels, or you could say in terms of different contexts, but whether the description is relevant depends on the question you ask or the problem you want to solve. [Pg.356]

Parasitology Research Group, School of Biology and Biochemistry, The Queen s University of Belfast, Medical Biology Centre, Belfast BT7 1NN, UK... [Pg.423]

In completing Phil s book we have retained the set of examples and explanations, and occasional commentary, as he had intended it. It has, however, been some time since a book on ESR for the non-expert has appeared. We have therefore supplemented his original manuscript in two ways. At the end of Chapter 1 is added an up-to-date list of texts and monographs on ESR which should serve the interested reader as a source of additional treatments of the subject. Secondly, in Appendix 2 we have referenced and given brief descriptions of some advanced ESR methods that have been developed in recent years and applied in various fields, including biochemistry. The modern ESR spec-troscopist is now as likely to need an understanding of these techniques as of the classic X-band methods described here. We hope that this book will provide a basis for study of the newer methods. [Pg.180]

Department of Chemistry and Biochemistry, The University of Mississippi, University, Mississippi 38677, USA... [Pg.275]

S. Bayne, Department of Biochemistry, The United College of St. Salvator and St. Leonard, The University, St. Andrews, Scotland... [Pg.469]

Techniques in biochemistry, the way they work, and what they tell you... [Pg.17]

The model most often invoked to rationalize cooperative behavior is the MWC (Monod-Wyman-Changeaux), or concerted, model. This model is 1.5 times more complicated than the Michaelis-Menten model and took three people to develop instead of two. Most texts describe it in detail. In the absence of substrate, the enzyme has a low affinity for substrate. The MWC folks say that the enzyme is in a T (for tense or taut) state in the absence of substrate. Coexisting with this low-affinity T state is another conformation of the enzyme, the R (for relaxed) state, that has a higher affinity for substrate. The T and R states coexist in the absence of substrate, but there s much more of the T state than the R. This has always seemed backward, since one would expect the enzyme to be more tense in the presence of substrates when some work is actually required. In keeping with the tradition of biochemistry, the MWC folks obviously wanted this to be backward too (Fig. 8-8). [Pg.132]

Table XI (346-390) lists a number of calcium-binding proteins and indicates very succinctly their role in biological systems. This table both illustrates the range of functions of calcium-binding proteins and serves to introduce those which appear subsequently in this chapter. The structures and functions of particularly important calcium-binding proteins such as calmodulin, parvalbumin, and troponin C are described in standard texts on biochemistry. The minimal Table XI entry for the particularly important calmodulins is amplified in the next paragraph. Table XI provides a sprinkling of references to enable readers to gain entry into the literature, for these and for most of the less-familiar species. Table XI (346-390) lists a number of calcium-binding proteins and indicates very succinctly their role in biological systems. This table both illustrates the range of functions of calcium-binding proteins and serves to introduce those which appear subsequently in this chapter. The structures and functions of particularly important calcium-binding proteins such as calmodulin, parvalbumin, and troponin C are described in standard texts on biochemistry. The minimal Table XI entry for the particularly important calmodulins is amplified in the next paragraph. Table XI provides a sprinkling of references to enable readers to gain entry into the literature, for these and for most of the less-familiar species.
In the context of ion channel biochemistry, and indeed in other areas of biochemistry, the term ligand has a different, and more... [Pg.365]

The fibroblasts do not convert cyanocobalamin or hydroxocobalamin to methylcobalamin or adenosyl-cobalamin, resulting in diminished activity of both N5-methyltetrahydrofolate homocysteine methyltransferase and methylmalonyl-CoA mutase. Supplementation with hydroxocobalamin rectifies the aberrant biochemistry. The precise nature of the underlying defect remains obscure. Diagnosis should be suspected in a child with homocystinuria, methylmalonic aciduria, megaloblastic anemia, hypomethioninemia and normal blood levels of folate and vitamin B12. A definitive diagnosis requires demonstration of these abnormalities in fibroblasts. Prenatal diagnosis is possible. [Pg.678]

Department of Chemistry and Biochemistry The University of Texas at Austin Austin, Texas... [Pg.4]

Department of Chemistry, University College London, Christopher Ingold Laboratories, London, WC1H OAJ, United Kingdom and Department of Chemistry and Biochemistry, The University of Texas at Austin, Austin, Texas, 78712... [Pg.10]

Kohler, Robert E. "From Medical Chemistry to Biochemistry The Making of a Biomedical Discipline" Cambridge University Press Cambridge, 1982. [Pg.30]


See other pages where Biochemistry: The is mentioned: [Pg.22]    [Pg.5]    [Pg.1129]    [Pg.388]    [Pg.424]    [Pg.145]    [Pg.5]    [Pg.1129]    [Pg.520]    [Pg.28]    [Pg.942]    [Pg.282]    [Pg.108]    [Pg.59]    [Pg.332]    [Pg.233]    [Pg.436]    [Pg.594]    [Pg.140]    [Pg.459]    [Pg.234]    [Pg.44]    [Pg.6]    [Pg.68]    [Pg.780]    [Pg.2]    [Pg.65]    [Pg.232]   


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