RESUMO
The muscle collagen of marine prawn, Penaeus indicus, was isolated by limited pepsin digestion. Based on selective salt precipitation, amino acid composition and gel electrophoretic pattern, the major collagen was found to be a homotrimer of á 1 chain, similar to type V collagen of vertebrates. Electron microscopy of reconstituted fibrils, made for the first time from a crustacean species, revealed a characteristic 64 nm periodicity. Biochemical studies indicate a less than normal amount of associated carbohydrates and an increased alanine content The major collagen had a denaturation temperature of 37°C with an intrinsic viscosity of 11·3 dl/g. Spectral characteristics of the major collagen were studied. Results suggest the presence of genetically distinct collagen types and acid resistant cross links in crustacean muscle.
RESUMO
Effects of oral and topical administration of an alcoholic extract of C. asiatica on rat dermal wound healing was studied. The extract increased cellular proliferation and collagen synthesis at the wound site, as evidenced by increase in DNA, protein and collagen content of granulation tissues. Quicker and better maturation and crosslinking of collagen was observed in the extract-treated rats, as indicated by the high stability of acid-soluble collagen and increase in aldehyde content and tensile strength. The extract treated wounds were found to epithelialise faster and the rate of wound contraction was higher, as compared to control wounds. The results show that C. asiatica produced different actions on the various phases of wound repair.