Biochemistry of Collagen
Gopalasamudram Ramachandran, G. N. Ramachandran, A. H. Reddi
Springer US, 1976 - Medical - 536 pages
Collagen is a fascinating protein not only because of its ubiquitous occurrence in multicellular animals, but also because of its unique chemi cal structure. As the predominant constituent in bone, cartilage, skin, tendon, and tooth, it is not surprising that collagen is of interest to anatomists, biochemists, biomedical engineers, cell biologists, dermatolo gists, dental surgeons, leather chemists, orthopedic surgeons, physiologists, physicians, zoologists, and a host of others. This book was planned to provide an up-to-date comprehensive survey of all aspects of biochemistry of collagen. The recent discovery of genetically distinct collagens with tissue specificity has opened a new era in collagen biochemistry, and Karl Piez discusses this in the opening chapter on primary structure. In the next chapter, Ramachandran and Rama krishnan deal with the molecular structure of collagen, placing special emphasis on the conformational aspects of its polypeptide chains. Follow ing the consideration of primary and secondary structure of collagen, the three-dimensional arrangement of collagen molecules in the fibrils is covered by Miller in Chapter 3. Collagen is generally in the insoluble state in the living organism due to the cross-linking of individual molecules, and Tanzer describes the various aspects of this cross-linkage in Chapter 4. The biosynthesis of collagen is discussed in depth by Prockop and his colleagues.
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Acta al(I Ala Ala Ala amino acid residues amino acid sequence antibodies antigenic antigenic determinants assay atoms axial Bailey band Biochem Biochemistry Biol Biophys biosynthesis bovine cells Chem chick embryo collagen fibrils collagen molecules collagenase collagenolytic connective tissue contain cross-links culture cyanogen bromide disulfide bonds electron micrographs enzyme evidence fibers fibroblasts Fietzek Figure Glimcher Gln Gln glycine helical Hosemann hydrogen bond hydroxylation hydroxylysine hydroxyproline Hyp Hyp Hyp interchain disulfide bonds intermolecular isolated Kivirikko lattice Lys Lys lysine lysyl lysyl hydroxylase Mechanic microfibril Miller molecular packing native collagen nonhelical observed occur peptide unit Piez polypeptide polypeptide chains position pro-o chains Proc procollagen proline prolyl hydroxylase protein purified rabbit Ramachandran rat skin reaction reflections region row lines skin collagen specific stability stained structure of collagen studies substrate synthesis tactoid Tanzer tendon tetragonal Timpl Traub triple helix triple-helical structure Udenfriend X-ray diffraction X-ray diffraction pattern