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

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

Collagen is an interesting protein not just as a result of its ubiquitous incidence in multicellular animals, but in addition due to its detailed chemi­ cal constitution. because the fundamental constituent in bone, cartilage, pores and skin, tendon, and enamel, it isn't fabulous that collagen is of curiosity to anatomists, biochemists, biomedical engineers, mobile biologists, dermatolo­ gists, dental surgeons, leather-based chemists, orthopedic surgeons, physiologists, physicians, zoologists, and a bunch of others. This publication used to be deliberate to supply an up to date complete survey of all points of biochemistry of collagen. the hot discovery of genetically distinctive collagens with tissue specificity has opened a brand new period in collagen biochemistry, and Karl Piez discusses this within the establishing bankruptcy on fundamental constitution. within the subsequent bankruptcy, Ramachandran and Rama­ krishnan take care of the molecular constitution of collagen, putting distinctive emphasis at the conformational features of its polypeptide chains. keep on with­ ing the honour of basic and secondary constitution of collagen, the third-dimensional association of collagen molecules within the fibrils is roofed by way of Miller in bankruptcy three. Collagen is usually within the insoluble kingdom within the dwelling organism a result of cross-linking of person molecules, and Tanzer describes a number of the elements of this cross-linkage in bankruptcy four. The biosynthesis of collagen is mentioned intensive through Prockop and his colleagues.

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Nothing is known about the formation or function of this amino acid. , 1963). , 1974; Cintron, 1974). This variability and its relationship to cross-linking is discussed elsewhere in this book (Chapters 4 and 8). It need only be noted here that only a few lysines appear to be fully hydroxylated in type I collagen of skin (residues 103, 697, 931, and 943, Table 1), although a number of other lysines are hydroxylated to a minor extent (Butler, 1968). Type II collagen, however, presents a different picture.

86 A per residue as in collagen. Since it seems unlikely that collagen triplet sequences could have arisen independently, the Clq sequence was compared to the al(I) sequence by computer techniques (Barker and Dayhoff, 1972) to look for a similarity that might be ascribed to homology. Although the 78 collagenlike residues (4-81, Figure 5) from Clq were found to be considerably more similar to residues 131-208 than to any other region in rat al(I), comparison to random triplet sequences indicates that the statistical significance is too low to support a common derivation (Piez, unpublished).

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. , Kang, A. , Toole, B. , 1972, Collagen heterogeneity. High resolution separation of native [al(I)]2a2 and [al(II)]3 and their component a chains,j. Biol. Chem. 247:6469. , 1971, Isolation and characterization of the cyanogen bromide peptides from the al and a2 chains of acid-soluble bovine skin collagen, Biochemistry 10:1751.

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