Biochemistry of Collagen - download pdf or read online

By Karl. A. Piez (auth.), G. N. Ramachandran, A. H. Reddi (eds.)

ISBN-10: 1475746024

ISBN-13: 9781475746020

ISBN-10: 1475746040

ISBN-13: 9781475746044

Collagen is an interesting protein not just due to its ubiquitous prevalence in multicellular animals, but in addition due to its specified chemi­ cal constitution. because the important constituent in bone, cartilage, dermis, tendon, and the teeth, it isn't spectacular that collagen is of curiosity to anatomists, biochemists, biomedical engineers, mobilephone biologists, dermatolo­ gists, dental surgeons, leather-based chemists, orthopedic surgeons, physiologists, physicians, zoologists, and a bunch of others. This booklet was once deliberate to supply an up to date complete survey of all elements of biochemistry of collagen. the new discovery of genetically exact collagens with tissue specificity has opened a brand new period in collagen biochemistry, and Karl Piez discusses this within the commencing bankruptcy on basic constitution. within the subsequent bankruptcy, Ramachandran and Rama­ krishnan take care of the molecular constitution of collagen, putting detailed emphasis at the conformational features of its polypeptide chains. stick with­ ing the glory of fundamental and secondary constitution of collagen, the three-d association of collagen molecules within the fibrils is roofed by means of Miller in bankruptcy three. Collagen is mostly within the insoluble nation within the residing organism as a result of the cross-linking of person molecules, and Tanzer describes many of the points of this cross-linkage in bankruptcy four. The biosynthesis of collagen is mentioned intensive by way of Prockop and his colleagues.

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J. , Parry, D. A. , Piez, K. , 1973, Analysis of the primary structure of collagen for the origins of molecular packing,]. Mol. Bioi. 79:137. PRIMARY STRUCTURE 43 Kang, A. , 1972, Studies on the location of intermolecular cross-links in collagen. Isolation of a CNBr peptide containing ll-hydroxylysinonorleucine, Biochemistry 11: 1828. Kang, A. , 1970, Amino acid sequence of cyanogen bromide peptides from the amino-terminal region of chick skin collagen, Biochemistry 9:796. Kang, A. , Dixit, S. , 1975, The covalent structure of collagen: Amino acid sequence of ai-CBS glycopeptide and al-CB4 from chick skin collagen,I Bioi.

Model properties of a natural protein antigen, Behring [nst. Mitt. 53:66. , 1969, The formation of triple-helical collagen molecules from al or a2 polypeptide chains, Eur. j. Biochem. 7:454. , and Piez, K. , 1971, The chemistry and structure of collagen, Adv. Prot. Chem. 25:243. Trelstad, R. , 1974, Human aorta collagens: Evidence for three distinct species, Biochem. Biophys. Res. Commun. 57:717. , Kang, A. , 1970, Isolation of two distinct collagens from chick cartilage, Biochemistry 9:4993. Trelstad, R.

1973, Biochemistry of collagens from mineralized tissues, in: Hard Tissue Growth, Repair and Rernineralization, pp. 247-261, ASP (Elsevier Excerpta Medica North-Holland), Amsterdam. Barnes, M. , Constable, B. , Morton, L. , and Royce, P. , 1974, Age-related variations in hydroxylation of lysine and proline in collagen, Biochem. I 139:461. , 1972, Cyanogen bromide peptides of the rabbit collagen alchain, FEBS Lett. 27:85. , 1967, Comparative sequence studies of rat skin and tendon collagen. I.

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Biochemistry of Collagen by Karl. A. Piez (auth.), G. N. Ramachandran, A. H. Reddi (eds.)


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