Purification and characterization of parvalbumins from silver carp (Hypophthalmichthy molitrix)

被引：27
作者：
Liu, Guang-Ming [1 ]
Wang, Ning [1 ,2 ]
Cai, Qiu-Feng [1 ,2 ]
Li, Teng [2 ]
Sun, Le-Chang [1 ]
Su, Wen-Jin [1 ]
Cao, Min-Jie [1 ]
机构：
[1] Jimei Univ, Coll Biol Engn, Key Lab Sci & Technol Aquaculture & Food Safety, Xiamen 361021, Peoples R China
[2] Shanghai Ocean Univ, Coll Food Sci, Shanghai 201306, Peoples R China
来源：
JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE | 2010年 / 90卷 / 06期
关键词：
silver carp; parvalbumin; purification; cDNA cloning; characterization; tricine SDS-PAGE; MAJOR ALLERGEN; FROG PARVALBUMIN; FISH; PROTEIN; HYPERSENSITIVITY; EXPRESSION; REACTIVITY; CLONING; IGE; COD;
D O I：
10.1002/jsfa.3913
中图分类号：
S [农业科学];
学科分类号：
09 ;
摘要：
BACKGROUND: As the largest producer and consumer of freshwater fish in the world, many people suffer from allergy for consuming freshwater fish in China. However, the allergen profiles of freshwater fish are rarely known. RESULTS: Parvalbumins (PVs) from the white muscle of silver carp (Hypophthalmichthy molitrix) were purified by ammonium sulfate fractionation and column chromatography including DEAE-Sepharose and Superdex 75. Three PV isoforms -PV-I, PV-II, and PV-III - were obtained and their molecular masses as estimated by tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis were 12, 11, and 14 kDa, respectively. All the PVs could be detected by anti-frog PV monoclonal antibody. PV-I and PV-II were quite possibly glycoproteins, while PV-III was not glycosylated, as analyzed by periodic acid-Schiff (PAS) staining. Thermal stability revealed that PV-I and PV-II easily formed polymers, while these proteins were stable in a pH range of 4.0-10.0. A PV gene encoding 110 amino acid residues was cloned and it revealed high identity with PVs from other species of fish. CONCLUSION: Three isotypes of PV were purified to homogeneity and one distinct PV gene was cloned in silver carp white muscle. (C) 2010 Society of Chemical Industry
引用
收藏
页码：1034 / 1040
页数：7
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