Please use this identifier to cite or link to this item: http://repository.ipb.ac.id/handle/123456789/77133
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dc.contributor.authorSantoso, Joko-
dc.contributor.authorIshizuka, Yuka-
dc.contributor.authorYoshie-Stark, Yumiko-
dc.date.accessioned2015-12-23T04:43:07Z-
dc.date.available2015-12-23T04:43:07Z-
dc.date.issued2012-
dc.identifier.urihttp://repository.ipb.ac.id/handle/123456789/77133-
dc.description.abstractThis experiment was carried out to determine the proximate composition of the mid-gut gland (MGG) of the Japanese scallop Patinopecten yessoensis to evaluate the characteristics of divalent minerals and water-soluble protein at various pHs, and to examine Cd-binding protein at different molecular weights. MGG of scallop contained protein, fat and ash of 28.9 g/100 g dry matter, 44.6 g/ 100 g dry matter and 6.78 g/100 dry matter, respectively. MGG also contained the macrominerals sodium, potassium, magnesium and calcium, and the trace minerals iron, zinc, cadmium and copper. The solubility of divalent minerals and water-soluble protein was high in both acidic and alkaline conditions, except that magnesium was not affected by acidity. The solubility of copper and iron had a positive correlation with water-soluble protein at all pH values, whereas cadmium had a strong correlation at alkaline pH. Low-molecular-weight water-soluble protein (fraction III, 437.5\MW\1,355) bound cadmium strongly in acidic, neutral and alkaline conditions. However, in acidic conditions cadmium had the strongest binding to protein.id
dc.language.isoenid
dc.publisherThe Japanese Society of Fisheries Scienceid
dc.relation.ispartofseries78:675–682;-
dc.titleCharacteristics of minerals extracted from the mid-gut gland of Japanese scallop Patinopecten yessoensis at various pH valuesid
dc.typeArticleid
dc.subject.keywordCadmiumid
dc.subject.keywordbinding proteinid
dc.subject.keywordJapanese scallopid
dc.subject.keywordMidid
dc.subject.keywordgut glandid
dc.subject.keywordMineralsid
dc.subject.keywordSolubilityid
dc.subject.keywordWater-soluble proteinid
Appears in Collections:Faculty of Fisheries and Marine Science

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