Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Hydroxyallysine"'
Autor:
Ruud A. Bank, Jeroen DeGroot, Anne-Marie Zuurmond, Annemarie J. van der Slot-Verhoeven, Tom W J Huizinga, Ernst A. van Dura, Joline Attema, Bep Blauw
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1740(1):60-67
Fibrotic processes in humans are characterised by an excessive accumulation of collagen containing increased levels of hydroxyallysine-derived cross-links. The occurrence of these cross-links appears to be an important criterion in assessing the irre
Publikováno v:
Journal of Biosciences. 15:289-295
To elucidate the biochemical basis of impaired skin collagen maturity in pyridoxine-or riboflavin-deficient rats the following two mechanistic possibilities were tested: (i) Reduction in the activity of skin lysyl oxidase (EC 1·4·3·13) which initi
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Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure. 336:100-107
The effect of heat on collagen cross-links has been studied using guinea pig dermal collagen and guinea pig scar collagen. Kinetic studies of heat solubilisation of bovine tendon indicated that covalent links were cleaved above 71 °C. Heat denaturat
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure. 405:412-421
The collagen produced in response to an injury of human skin is initially stabilized by a cross-link derived from hydroxyallysine, and characteristic of embryonic skin. In normal healing there is a change over with time to the cross-link derived from
Publikováno v:
Biochemical and biophysical research communications. 67(2)
A new trifunctional crosslink, termed hydroxyaldol-histidine, was isolated from cow skin collagen. This compound was not reducible by sodium borohydride; it was characterized by PMR spectroscopy and by low and high resolution mass spectroscopy of vol