The relationship between the degree of hydroxylation and oxidative deamination of e-NH2-groups of lysine and hydroxylysine in collagen, and the thermal stability of this protein’s sub-molecular structures in the skin of Wistar rats in their postnatal ontogeny was in vitro studied. It has been shown ...
The relationship between the degree of hydroxylation and oxidative deamination of e-NH2-groups of lysine and hydroxylysine in collagen, and the thermal stability of this protein’s sub-molecular structures in the skin of Wistar rats in their postnatal ontogeny was in vitro studied. It has been shown that, rising towards the age of 3 months, the content of free e-NH2-groups in collagen continuously remains constant, while that of free aldehyde groups (COH-groups), starting from 1-month steadily decreases with age. Accordingly, intermolecular cross-linking in collagen’s sub-molecular structures is reduced during the period between 1 to 3 months, and afterwards continuously increases up to 24 months of age. The content of hydroxyproline in collagen is continuously reduced in postnatal ontogenesis. The combined effect of both effects leads to a decrease in the thermal stability of collagen sub-molecular structures in the skin during the period from 1 to 3 months, and subsequently rises up to 24 months old.
El-ta'alu A B, Persky, Eu E, Bulankina Na I, Kot Yu G, Kot Ek V, Ponomarenko Al N, Kostina Ta V. The Role of Collagen Processing in Age-related Changes in the Thermo-stability of Connective Tissue Macromolecule - Collagen . WebmedCentral BIOCHEMISTRY 2011;2(11):WMC002392