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dc.contributor.authorMontero García, Pilar-
dc.contributor.authorBorderías, A. Javier-
dc.contributor.authorTurnay, J.-
dc.contributor.authorLeyzarbe, M. Antonia-
dc.date.accessioned2013-02-08T08:28:56Z-
dc.date.available2013-02-08T08:28:56Z-
dc.date.issued1990-
dc.identifierissn: 0021-8561-
dc.identifier.citationJournal of Agricultural and Food Chemistry 38: 604- 609 (1990)-
dc.identifier.urihttp://hdl.handle.net/10261/66346-
dc.description.abstractAn analysis of the different types of collagen present in various body structures, the amino acid composition of the collagen, and the degree of collagen aggregation for hake and trout is presented. Type I collagen was found at all body sites, and its amino acid profile and degree of hydroxylation are considered. Hydroxyproline values, the ratio of hydroxyproline to the other amino acids, and the proportions of alanine, tyrosine, and methionine are also discussed. Values for collagen solubility in salt and acid indicated a lower insolubility rate for skin collagen than for muscle collagen. The proportions of the α, β, and γ components in the acid-soluble fractions of skin and muscle collagen are also examined; the proportion of γ components is lower in hake muscle collagen than in hake skin collagen, whereas the converse holds true in trout. © 1990 American Chemical Society.-
dc.language.isoeng-
dc.publisherAmerican Chemical Society-
dc.rightsclosedAccess-
dc.titleCharacterization of hake (Merluccius merluccius L.) and trout (Salmo irideus Gibb) collagen-
dc.typeartículo-
dc.date.updated2013-02-08T08:28:56Z-
dc.description.versionPeer Reviewed-
Appears in Collections:(ICTAN) Artículos
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