Abstract
The effect in vitro of nitrogen mustard (HN2) on physical parameters of rat tail tendon collagen and rabbit skin collagen was studied. Intrinsc viscosities, helix-coil transition temperatures (by viscosimetry and rates of fibril formation (by turbidimetry) of HN2-treated (1 mg/ml HN2, 0·.9% saline, 2 hr at 25°) and control collagens were compared. Helix-coil transition temperatures were not affected by HN 2 treatment. Fibril formation by both collagens was inhibited by HN 2, but apparently this effect was nonspecific since it was reversible by dialysis. Rat tail tendon collagen aggregates in solution were disaggregated by HN 2 treatment. Only 0·5 per cent of the hydroxyproline of collagen became dialyzable after HN 2 treatment.
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