{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1361981471410071808.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1016/s0308-8146(01)00396-x"}},{"identifier":{"@type":"URI","@value":"https://api.elsevier.com/content/article/PII:S030881460100396X?httpAccept=text/xml"}},{"identifier":{"@type":"URI","@value":"https://api.elsevier.com/content/article/PII:S030881460100396X?httpAccept=text/plain"}}],"dc:title":[{"@value":"Collagen of the skin of ocellate puffer fish (Takifugu rubripes)"}],"description":[{"notation":[{"@value":"Abstract   Collagens (acid-solubilized and pepsin-solubilized collagens) were prepared from ocellate puffer fish skin and partially characterized. With respect to the pepsin-solubilized collagen, it was a heterotrimer with a chain composition of (α1) 2 α2. The patterns of peptide fragments were different from skin collagens of other species. The denaturation temperature was 28 °C, about 9 °C lower than that of porcine skin collagen. On the other hand, the yields of acid-solubilized and pepsin-solubilized collagens were very high, 10.7% and 44.7%, respectively, on a dry weight basis. These results suggest that ocellate puffer fish skin has potential as an alternative source of collagen for use in various fields."}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1381981471410071810","@type":"Researcher","foaf:name":[{"@value":"Takeshi Nagai"}]},{"@id":"https://cir.nii.ac.jp/crid/1381981471410071809","@type":"Researcher","foaf:name":[{"@value":"Yoko Araki"}]},{"@id":"https://cir.nii.ac.jp/crid/1381981471410071808","@type":"Researcher","foaf:name":[{"@value":"Nobutaka Suzuki"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"03088146"}],"prism:publicationName":[{"@value":"Food Chemistry"}],"dc:publisher":[{"@value":"Elsevier BV"}],"prism:publicationDate":"2002-08","prism:volume":"78","prism:number":"2","prism:startingPage":"173","prism:endingPage":"177"},"reviewed":"false","dc:rights":["https://www.elsevier.com/tdm/userlicense/1.0/"],"url":[{"@id":"https://api.elsevier.com/content/article/PII:S030881460100396X?httpAccept=text/xml"},{"@id":"https://api.elsevier.com/content/article/PII:S030881460100396X?httpAccept=text/plain"}],"createdAt":"2002-10-14","modifiedAt":"2019-05-03","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1050869456405284608","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"The effect of alkaline pretreatment on the biochemical characteristics and fibril-forming abilities of types I and II collagen extracted from bester sturgeon by-products"}]},{"@id":"https://cir.nii.ac.jp/crid/1360283690905504512","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Isolation and characterization of acid-soluble collagen from the scales of marine fishes from Japan and Vietnam"}]},{"@id":"https://cir.nii.ac.jp/crid/1360846640858968832","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Biochemical characterisation and assessment of fibril-forming ability of collagens extracted from Bester sturgeon Huso huso×Acipenser ruthenus"}]},{"@id":"https://cir.nii.ac.jp/crid/1361975845616880896","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Biochemical study of type I collagen purified from skin of warm sea teleost Mahi mahi (\n            <i>Coryphaena hippurus</i>\n            ), with a focus on thermal and physical stability"}]},{"@id":"https://cir.nii.ac.jp/crid/1390001204459801984","@type":"Article","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Isolation and Characterization of Pepsin-Soluble Collagen from Abalone (<i>Haliotis discus hannai</i>) Gastropod Muscle Part II"},{"@value":"Isolation and Characterization of Pepsin-Soluble Collagen from Abalone (Haliotis discus hannai) Gastropod Muscle Part II"}]},{"@id":"https://cir.nii.ac.jp/crid/1880302167595844352","@type":"Dataset","relationType":["references","isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Quality control for modern bone collagen stable carbon and nitrogen isotope measurements"}]}],"dataSourceIdentifier":[{"@type":"CROSSREF","@value":"10.1016/s0308-8146(01)00396-x"},{"@type":"OPENAIRE","@value":"doi_dedup___::4466886e31a01c1d8b3e8b9e5f381c2e"},{"@type":"CROSSREF","@value":"10.1016/j.foodchem.2013.10.094_references_DOI_HSj7Yq6b9BySOT2I8FTUw5A9AMM"},{"@type":"CROSSREF","@value":"10.3136/fstr.18.271_references_DOI_HSj7Yq6b9BySOT2I8FTUw5A9AMM"},{"@type":"CROSSREF","@value":"10.1016/j.ijbiomac.2019.03.091_references_DOI_HSj7Yq6b9BySOT2I8FTUw5A9AMM"},{"@type":"CROSSREF","@value":"10.1016/j.foodchem.2014.03.075_references_DOI_HSj7Yq6b9BySOT2I8FTUw5A9AMM"},{"@type":"CROSSREF","@value":"10.1111/jfbc.13013_references_DOI_HSj7Yq6b9BySOT2I8FTUw5A9AMM"}]}