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Title: シャコの微量元素結合タンパク質及びタンパク質の分離とその性質に関する研究
Other Titles: Isolation and Characterization of Trace Element-Bounding proteins and phosphonoproteins from Squilla oratoria
Authors: 玉利, 正人 / 池田, まどか
Authors (alternative): Tamari, Masato / Ikeda, Madoka
Issue Date: 28-Feb-1987
Publisher: 長崎大学教育学部
Citation: 長崎大学教育学部自然科学研究報告. vol.38, p.61-72; 1987
Abstract: (1) We describe a method of extraction and partial purification of phosphoproteins and phosphonoproteins isolated from Squilla oratoria. The extraction of these proteins was carried out by 0.02M NaHCO3 solution containing 5% NaCl or by hot water. It has been demonstrated that Squilla oratoria was contained four hot water soluble proteins and three alkaline soluble proteins. The phosphoproteins and phosphonoproteins were found in the hot water soluble proteins and in the alkaline soluble proteins, respectively. (2) The amino acid compositions of the each samples were characterized by relatively high percentages for glutamic acid and glycine, which conforms to amino acid composition of lobster in other shellfish. It has been found that free amino acids occurs the large amount in the outer solution by dialysis of the alkaline extracts. (3) Mineral contents (Fe, Ca, Zn) in Squilla oratoria was found about 40% as insoluble materials in the residues and about 45-50% as low molecular-bounding-form or free-form in the water soluble fraction. Further, it has been found that Ca occurs as alkaline soluble low molecular-bounding-form or free-form and that Fe and Zn occurs as insoluble complex-form. (4) It has been demonstrated that the peak E contained the highest concentration of phosphonoproteins and that about 85% of organic phosphorus occurs as phosphonate-phosphorus. Further, peak E was formed four peptides by tryptic digestion. The amino acid composition of these peptides showed a high glutamic acid, glycine, lysine, phenylalanine and tyrosine content.
URI: http://hdl.handle.net/10069/32493
ISSN: 0386443X
Type: Departmental Bulletin Paper
Text Version: publisher
Appears in Collections:No. 38

Citable URI : http://hdl.handle.net/10069/32493

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