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Amino acids comparative biochemistry

Levine, P. T., Seyer, J. M., Huddleston, J., Glimcher, M. J. The comparative biochemistry of the organic matrix proteins of the developing enamel I. Amino acid composition. Arch, oral Biol. 12, 407 (1967)... [Pg.130]

Biochemical evolution refers to changes over geologic time of the fundamental composition of organic components—e.g., the sequence of amino acids in protein molecules. The best documented example of biochemical evolution is that of the respiratory pigment haemoglobin, and the relation of its evolution to the fossil record has been summarized recently (58). Many of the monographs on comparative biochemistry have discussed biochemical evolution (59, 60, 61), and the reader is... [Pg.41]

Radzika, A., Wolfenden, R. (1988) Comparing the polarities of the amino acids Side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol and neutral aqueous solution, Biochemistry 27, 1664-1670 ... [Pg.302]

Cowey, C.B., Daisley, K.W. and Parry, G. (1962). Study of amino acids, free or as components of protein, and of some B vitamins, in the tissues of the Atlantic salmon, Salmo salar, during spawning migration. Comparative Biochemistry and Physiology 7,29-38. [Pg.266]

Gur yanova, S. D. (1977). [The amino-acid composition of the total proteins of plerocercoids of the genus Diphyllobothrium and their hosts.] In Russian. In [Comparative biochemistry of fish and their helminths. Lipids, enzymes, proteins. (Collected uwfcy).] ed. V. S. [Pg.322]

Mettrick, D. F. (1970). Protein nitrogen, amino acid and carbohydrate gradients in the rat intestine. Comparative Physiology and Biochemistry, 37 517-41. [Pg.338]

Wack, M Komuniecki, R. Roberts, L. S. (1983). Amino acid metabolism in the rat tapeworm, Hymenolepis diminuta. Comparative Biochemistry and Physiology, 74B 399-402. [Pg.364]

My second comment is apropos of Channing Robertson s remarks, which I admired. In regard to polymers, it seems to me that the time has come to adopt again a unifying approach like that of Charles Tanford, professor of biochemistry at Duke University, who wrote the book Physical Chemistry of Macromolecules comparing biopolymers with synthetic polymers. In polymer synthesis, let s look at the synthesis of peptides, amino acid by amino acid, and the desynthesis of peptides by sequencing, and bring this into our curriculum. [Pg.491]

Separation of amino acids and their identification in different mixtures are frequent tasks encountered in biochemistry. Thin layer chromatography is a fast, simple, and inexpensive approach to attain this goal. Because some of the components are UV-inactive, other methods, such as vibrational spectroscopy, should be applied for detection and identification. Comparative study based on Raman spectroscopy of thin layer chromatography spots of some weak Raman scatterers (essential amino acids) was carried out using four different visible and near-infrared laser radiation wavelengths 532, 633,785, and 1064 nm. The best results were obtained with simple silica gel plates. [Pg.1086]

This method is already relatively old and has been used for the past several years in organic chemistry and biochemistry. High kinetic energy (several keV) primary ions, e.g., Ar, bombard a surface on which the sample has been deposited. Under these conditions, ions are extracted from the surface and can be analyzed, Benninghoven and co-workers [102] presented a number of examples carbohydrates, alkaloids, amino acids (and derivatives) and peptides. As with the other methods, both positive and negative ionization modes are possible (Fig. 14). More recently, the same author [103] demonstrated the possibility of studying non-volatile nucleic acids and compared the results obtained with the other desorption methods. Sensitivity limits are on the order of ng. [Pg.165]

Similarity of Proteins. When proteins are compared to find whether they are In the same group, their similarity can be tested In two aspects. One Is protein function proteins that are Identical In their catalytic functions have the same enzymatic name and EC-number given by the International Union of Biochemistry (lUB). The other way of grouping Is based on amino acid sequence. Proteins of similar sequences are classified Into the same group. [Pg.107]

Although higher plants being autotrophs are not dependent on external organic compounds for existence, the use of labeled substrates has shown that they are capable of many of the catabolic reactions found in other organisms. This chapter will examine the catabolism of the protein amino acids in this context of comparative biochemistry. [Pg.542]

Tandem mass spectrometry (MS/MS) is very useful for the amino acid sequencing of peptides, and has been used widely in both protein biochemistry and pro-teomics to identify proteins, to deduce the sequence of a peptide, and to detect and locate post-translational modifications. Until around a decade ago, the concept of amino acid sequencing by MS-technologjes was synonymous with ESI-MS/MS, but today MALDI-MS/MS techniques are implemented in high-performance instruments such that the quality of MALDI tandem mass spectra is comparable with that of ESI-MS/MS spectra. Currently, MALDI tandem mass spectrometers exist in a number of geometries, including TOF-TOF, Q-TOF, ion trap and orbitrap analyzers that each provide unique analytical features for the sequencing of peptides and proteins by MS/MS (details of the instrumentation for different types of MS/MS are provided in Chapter 2). [Pg.108]


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