Purification and partial characterization of a type V like collagen from the muscle of marine prawn, Penaeus indicus.

dc.contributor.authorSivakumar, V P
dc.contributor.authorSuguna, L
dc.contributor.authorChandrakasan, Gowri
dc.date.accessioned2015-08-01T04:20:52Z
dc.date.available2015-08-01T04:20:52Z
dc.date.issued1997-03
dc.description.abstractThe 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.en_US
dc.identifier.citationSivakumar 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.en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/161103
dc.language.isoenen_US
dc.source.urihttps://www.ias.ac.in/jarch/jbiosci/22/131-141.pdfen_US
dc.subjectCrustacean type V collagenen_US
dc.subjectfibrillogenesisen_US
dc.subjectphysico-chemical propertiesen_US
dc.subjectUV and IR spectraen_US
dc.titlePurification and partial characterization of a type V like collagen from the muscle of marine prawn, Penaeus indicus.en_US
dc.typeArticleen_US
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