Abstract
Both the rate and the extent of reactivity of carbonyl groups of α-collagen fractions of acetic acid extracted skin collagen of aminonucleoside-nephrotic (AN) rats are reduced in comparison with the reactivity of such groups in similar fractions prepared from normal rat skin. Since collagen fibrillogenesis is dependent upon the participation of such groups in the formation of both intra- and intermolecular cross-linkages, differences might be expected to be demonstrable between the ultrastructure of collagen fibrils reconstituted from solubilized preparations of skin collagen from the normal and the AN rats. To investigate this possibility, skin collagen from both normal and AN rats was prepared essentially as described by Gross and Kirk. The collagen was solubilized in each case in 0.2M acetic acid and then dialized against 0.2M NaCl for four days at 4°C. Collagen fibrils reconstituted in this manner were negatively stained for electron microscopy with 1 percent phosphotungstic acid adjusted to pH with NaOH.
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Schedule a callMore From: Proceedings, annual meeting, Electron Microscopy Society of America
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