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SOLID PHASE PEPTIDE SYNTHESIS --- PEPTIDES --- PEPTIDES --- ANALYSIS --- PREPARATION --- SOLID PHASE PEPTIDE SYNTHESIS --- PEPTIDES --- PEPTIDES --- ANALYSIS --- PREPARATION

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Antisense nucleic acids --- Antisense peptides

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How do you keep track of basic information on the proteins you work with? Where do you find details of their physicochemical properties, amino acid sequences, gene organization? Are you tired of scanning review articles, primary papers and databases to locate that elusive fact? The Academic Press FactsBook series will satisfy scientists and clinical researchers suffering from information overload. Each volume provides a catalog of the essential properties of families of molecules. Gene organization, amino acid sequences, physicochemical properties, and biological activity are presen

Chemokines --- Cytokines. --- Chemotactic cytokines --- Inflammatory peptides --- Intercrines --- Cellular immunity --- Immune response --- Cytokines --- Inflammation --- Peptides --- Regulation --- Mediators

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Neuropeptide Y (NPY) is a ubiquitous and important messenger in the nervous system, with a wide range of physiological roles. It is involved in the body energy balance and is one of the most potent stimuli of food intake known. NPY also acts to regulate central and peripheral autonomic functions.This book, written by academic and industrial experts in the field, links the most recent basic experimental knowledge about NPY and its receptors with areas of clinical importance.This book will be of interest to those working in all areas of research affected by NPY, such as food intak

Neuropeptide Y. --- Neuropeptides. --- Brain peptides --- Nerve tissue proteins --- Neurotransmitters --- Peptides --- Neuropeptide tyrosine --- NPY (Neuropeptide) --- Neuropeptides

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The purpose of this work was to prepare a peptidic product from milk proteins which is devoid of phenylalanine (Phe) and whose organoleptic qualities are considerably better than those of currently available products ; it is designed for use in the nitrogen supply of phenylketonurics (PKU). To achieve that purpose, we decided to isolate the caseinophosphopeptides (CPP), i. e. large tryptic peptides, containing very little Phe. Two separation methods were tested, one using phosphocalcic aggregation followed by precipitation in alcohol and the other phosphocalcic aggregation followed by ultrafiltration. We obtained peptides containing 4 to 5 times less Phe than the initial peptides (1 % against 4.7 %) ; compared with casein, yields of between 9.9 to 13 % were reached, depending on the raw material chosen (sodium caseinate or skimmed milk). A third separation and purification method was also tested, using anion exchange chromatography (3 resins). It was adjusted for use in semi-preparations. Calculation of the loads and the isoelectric points of the CPPs enabled selection of a buffer pH able to eliminate not only the non-phosphorylated peptides (with Phe) but also the three CPP, each still containing a Phe residue. This resulted in a product made up long, Phe-free peptides (0.1 to 0.2 % max). In comparison with casein, the average yields were 5.9 to 7.0 % of CPP, depending on the initial substrate. The yields are fairly low but the resulting products contain no free amino acids and are not bitter. After further hydrolysis, the other tryptic peptides can be used in special hyperprotein diets or in semi-elementary diets.

Milk protein --- Milk protein --- peptides --- peptides --- Hydrolysis --- Hydrolysis --- Amino acids --- Amino acids --- Separating. --- Separating