Chemistry of natural protein fibers - download pdf or read online

By R. S. Asquith

ISBN-10: 0306308983

ISBN-13: 9780306308987

This quantity arose initially from the proceedings of the editor's scholars, either undergraduate and postgraduate, that there has been no smooth publication on protein fibers which informed sufficient approximately protein technological know-how and chemical tech­ nologies regarding fibers. mainly this can be most likely a cheap cri de coeur. The undergraduate on a technological path, missing info at the uncomplicated medical innovations used to hold out the examine on which his fiber expertise relies, can locate it tricky to acquire this data. The natural technological know-how undergraduate usually lacks wisdom of the applying of those concepts in protein fiber know-how. The younger graduates, com­ mencing examine concerning a few point of protein fibers, are drawn from quite a lot of medical disciplines, having been expert as biochemists, chemists, physicists, technologists, and histologists, to call yet a couple of. more often than not those new learn employees go through a initial "lost" interval within which they need to overview their historical past on the subject of the huge and differing fields of analysis in protein fiber technological know-how to which they're now uncovered. As time is going on they then both enhance a large wisdom masking technology and know-how or stay in a particular a part of their unique self-discipline, with a slender wisdom of its software within the box of the examine measure they're taking.

Show description

Read or Download Chemistry of natural protein fibers PDF

Best biochemistry books

New PDF release: Molecular Mechanisms of Microbial Adhesion: Proceedings of

It's been eighty years because the topic of bacterial adhesion to surfaces was once first introduced forth, yet merely within the final twenty years has the significance of this topic been well-known via clinical microbiologists. the truth that bacterial attachment to the host tissue is a prerequisite for an infection understandably ended in the wish that infections will be avoided by means of blocking off the adhesion of pathogenic micro organism.

Electron Paramagnetic Resonance in Biochemistry and Medicine - download pdf or read online

Electron Paramagnetic Resonance (EPR) spectroscopy - additionally occasionally termed Electron Spin Resonance spectroscopy - has manifold capability makes use of in biochemistry and medication. The paramount value of EPR spectroscopy utilized to organic tissues and fluids is that it identifies the alterations in redox tactics that give a contribution to affliction.

Extra info for Chemistry of natural protein fibers

Sample text

Most other methods are based on the oxidation of lanthionine to its sulfoxide, which facilitates separation. 4. Cysteic Acid The cysteic acid content of wool is an index of oxidative treatment undergone by the fiber, and its determination is of some technological importance. Ziegler(132) and Bauters et al. (133) discuss the problem and describe methods based on paper electrophoresis. 5. 1), it is frequently desirable to obtain the total amide value by less elaborate means. Leach and Parkhill (135) showed that liberation of ammonia from amide groups was complete after hydrolysis with 12 N hydrochloric acid at 37°C for 10-12 days.

3. Location of Disulfide Bridges The pairing of half-cystine residues is usually the last step in the determination of the primary structure of a protein. It requires the isolation of 38 J. C. Fletcher and J. H. Buchanan peptides containing intact disulfide bonds, which are then cleaved, usually by oxidation, and the component cysteic acid-containing peptides separated, characterized, and located in the known primary structure. 4). 7) for the visualization of cystine peptides on peptide maps has been described by Glaser et al.

Cleavage by Enzymes Acting on Modified Proteins A useful extension of the technique of digestion with enzymes of high specificity is afforded by chemical modification of amino acid side chains. Thus trypsin, which acts at peptide bonds involving arginine or lysine residues, can be restricted to act at only one of these types of residue if the other is chemically modified so that its side chain no longer fulfils the specificity requirements of the enzyme. Further, if the chemical modification can be reversed, the high specificity of trypsin can be utilized again to split the peptides separated from the first digest, after the modifying group has been removed.

Download PDF sample

Chemistry of natural protein fibers by R. S. Asquith

by George

Rated 4.19 of 5 – based on 36 votes