Download Connective Tissue: Macromolecular Structure and Evolution by Professor Martin B. Mathews Ph. D. (auth.) PDF

By Professor Martin B. Mathews Ph. D. (auth.)

This ebook bargains essentially with the relevant extracellular macromole­ cules of animal connective tissues. It makes an attempt to respond to a few basic questions on the organic association of the tissues: what's the nature of this association at numerous dimensional degrees? What capabilities does the association serve? How has it developed? i've got given significant emphasis to the buildings and houses of the macromolecular elements of extracellular matrices from quite a lot of invertebrates and vertebrates. In doing so, notwithstanding, i've got handled cursorily many vital facets of connective tissue biology that looked to be in simple terms not directly proper to the imperative questions requested. nonetheless, i have never hesitated to go looking for vast organic ideas outdoors the present conceptual obstacles of animal connective tissues and the reduce molecular dimensional degrees. the various speculations offered will, i am hoping, stimulate the reader to extra concept and research. Acknowledgements My formerly unpublished info which were incorporated during this quantity couldn't were received with no the beneficiant presents of specimens and different counsel through a couple of contributors and associations. those are Dr. G. BERENSON of Louisiana nation collage, Drs. W. P. BRAKER and D. ZUMWALD of the Shedd Aquarium, Dr. S. H. CHUANG of the Univer­ sity of Singapore, Dr. L. G. CLARK and Mr. U. M. VARELA-DIAZ of the college of Pennsylvania, the govt of Nicaragua, Dr. E. CLARK of Cape Haze Marine Laboratories, Mr. C. E.

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Additional resources for Connective Tissue: Macromolecular Structure and Evolution

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However, only a portion of the structure is likely to be in the triple helical conformation (LUCAS and RUDALL, 1968). The insoluble tissue residue of a crustacean, the white shrimp Penaus setiferous. gave a wide-angle X-ray diffraction pattern typical of collagen (THOMPSON and THOMPSON, 1968, 1970). This residual "collagen" contained only 150 residues of glycine per 1000. While hexose was virtually absent, the tryptophan content of 119 residues per 1000 was extraordinarily high. It is apparent from the very low glycine contents that only a portion of the preparations of these authors consisted of collagen.

MILLER et al. (1969) found chick-bone "telopeptide" lysine to be hydroxylated to the extent of about 50% whereas skin "telopeptide" lysine remains unhydroxylated. , 1971; STOLTZ, FURTHMAYER and TIMPL, 1973). Collagens of human articular and costal cartilage are hydroxylated to a greater degree than dermal collagen. Basement-membrane collagens are characteristically very high in hydroxylysine. Hydroxylation is determined by many factors, including primary structure. , 1973) in vertebrates, but not in invertebrates (see Annelida, Sect.

An identical glycopeptide region was shown by BUTLER (1970) to be present in ratskin collagen (see Fig. 2) and by MORGAN et al. (1970) to be present in collagens of carp and man. MORGAN and coworkers also found an additional major glycopeptide in carp and human collagens with the structure Gly-Ile-Hyl(Gal-Glc)-Gly-His-Arg and Gly-Phe-Hyl(Gal-Glc)Gly-Ile-Arg for carp swim bladder collagen and human skin collagen, respectively. , 1973) emphasizes a narrow substrate specificity for the glycosylation process.

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