Purification and partial characterization of a type V like collagen from the muscle of marine prawn, Penaeus indicus.
Date
1997-03
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Abstract
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.
Description
Keywords
Crustacean type V collagen, fibrillogenesis, physico-chemical properties, UV and IR spectra
Citation
Sivakumar V P, Suguna L, Chandrakasan Gowri. Purification and partial characterization of a type V like collagen from the muscle of marine prawn, Penaeus indicus. Journal of Biosciences. 1997 Mar; 22(2): 131-141.