Methods in Enzymology Vol.144 Structural and Contractile Proteins, Part D: Extracellular Matrix

This chapter emphasizes on new developments concerning the relatively well-characterized collagens as well as on studies describing the more recently discovered collagens. It is abundantly clear that although collagen molecules function primarily as components of supporting aggregates, they constitute a large family of proteins with a wide spectrum of chemical and structural features. The nature of the aggregates derived from various types of molecules reflects this diversity. The molecular diversity of the collagen family of proteins is, of course, specified ultimately by the various genes utilized in synthesizing different collagen chains. The genetic heterogeneity is, however, considerably amplified through intracellular posttranslational modifications of the nascent chains as well as through extracellular processing of secreted molecules. A number of factors have greatly facilitated the acquisition of data on most of the collagens described above. Use of limited proteolysis with pepsin to facilitate the release of fragments of the molecules is one of these factors. Fragmentation of the molecules constitutes a serious limitation when this approach is utilized. However, it appears likely that many of the collagens for which extensive data are now available would have remained undetected were it not possible to isolate their fragments by means of limited proteolysis.

• Hardcover: 561 pages
• Publisher: Academic Press;
  
• Language: English
• ISBN-10: 0121820440
• ISBN-13: 978-0121820442
• Product Dimensions: 6 x 9 inches

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