Collagen small

The media is composed of diagonally oriented smooth muscle cells. They are surrounded by collagen, small elastic fibers, and glycosaminoglycans (proteoglycans). Most cells are attached to one another by specific junctional complex, which are arranged as spirals between the elastic fibers and support the arterial wall. 

The collagen small-angle layer lines are remarkable for their sharpness, i.e., their small breadth in the meridional direction, and their large... 

The collagen small-angle diffraction is, however, much more highly developed in terms of the number and sharpness of layer lines than is that of the synthetic fibers. While in the latter the large spacings are a sort of crystallization artifact, with the collagens the large structures are clearly related to complex chemical structure. 

The fifteen samples analyzed for amino acid composition were compared to a human type 1 collagen standard. There are no significant differences in amino acid composition among these samples, which range in age from stillbirth to adult. Analytical error is 10%. All samples show the typical composition of type 1 collagen (Table 1.1). Based on these results there is no reason to suspect differential preservation of specific amino acids in the small bones of infants in comparison to bones of adults and older children. 

The diet of the 19 century residents of Upper Canada was determined from historical sources and was reproduced in order to carry out chemical analysis. Stable carbon isotope analysis of food and human bone demonstrates that the spacing between the food eaten and the bone collagen is around 5.6%o. The value may vary slightly from this estimate since the latter is based on a reconstructed diet and a large number of bone samples, which exhibit a small amount of variation. Nevertheless, this empirically derived result agrees well with estimates from field (Vogel 1978), and laboratory studies (reviewed in Ambrose 1993). 

Figure All.l. A plot of the difference (residuals) between observed collagen 5 C values and values calculated from the DIFF for dp = +5, dn = +2, and f(F) = F , as a function of the dietary protein carbon content. Due to the eombination of eomposition and manipulated isotopic compositions of the different diets, some diets test the predictions of the DIFF more precisely than others. These are represented as squares (the remainder are represented as diamonds). Although the differenee has been minimized, it is not zero. Nevertheless, and especially for the more reliable reetangular points, the differenee is small, for a wide range of diets and collagen 8 values. Other combinations of dp, ds. and 1(F) give greater residuals.

There are approximately 200 other proteins present in bone, though most of them are present only in trace amounts (Delmas et al., 1984 Linde et al., 1980, as cited in van Klinken, 1991). The second most common bone protein, osteocalcin, comprises 1-2 weight % of total fresh bone. Osteocalcin bonds with both the bone mineral fraction and bone collagen, but it seems to be unstable in solutions. Due to its small molecular size and strong mineral stabilization, osteocalcin can survive up to 50.000 years (C.l. Smith et al., 2005), and it may offer an alternative to the use of collagen in paleoenvironmental stable isotope research. However, osteocalcin s role and importance in this field of study has yet to be defined (Collins et al., 2002). 

Collagen, the major component of most connective tissues, constimtes approximately 25% of the protein of mammals. It provides an extracellular framework for all metazoan animals and exists in virmally every animal tissue. At least 19 distinct types of collagen made up of 30 distinct polypeptide chains (each encoded by a separate gene) have been identified in human tissues. Although several of these are present only in small proportions, they may play important roles in determining the physical properties of specific tissues. In addition, a number of proteins (eg, the Clq component of the complement system, pulmonary surfactant proteins SP-A and SP-D) that are not classified as collagens have... 

The protein collagen undergoes hydrolytic degradation to gelatin in a manner which indicates the presence of a small minority of comparatively easily hydrolyzable bonds. Scatchard, Oncley, Williams, and Brown concluded that these are regularly spaced at intervals of about 1200 units in the collagen molecule. 

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