Purification and Characterization of Parvalbumin Isotypes from Japanese Flounder (Paralichthys olivaceus)

doi:10.7506/spkx1002-6630-20180706-084

Abstract

Abstract: Parvalbumins were extracted and purified from the muscle of Japanese flounder (Paralichthys olivaceus). A mixed solution of Tris, glycine, and DL-dithiothreitol was used as the extraction solvent. Parvalbumins were purified by adding ammonium sulfate to different degrees of saturation, and then identified using enzyme-linked immunosorbent assay (ELISA), Western-blot and high performance liquid chromatography-tandem mass spectrometry (HPLC-MS/MS). Three proteins (PVI, PVII and PVIII) with different molecular masses were obtained with high purity ( > 90%). Serological results demonstrated that each of these parvalbumins had the ability of binding to the specific IgG and IgE. The molecular masses of PVII and PVIII were determined to be 12 151 and 11 645 Da with Isoelectric point (pI) of 5.14 and 4.69, respectively. This method can meet the requirements for the extraction and purification of parvalbumins. These proteins were proved to represent different isotypes of parvalbumins with allergenicity.

Key words: fish allergen, parvalbumin isotypes, Japanese flounder, purification, identification

CLC Number:

TS254.1

SUN Lirui, LIN Hong, LI Zhenxing, ZHAO Jinxia, LIN Hang, LUO Chen, TIAN Shenglan. Purification and Characterization of Parvalbumin Isotypes from Japanese Flounder (Paralichthys olivaceus)[J]. FOOD SCIENCE, 2019, 40(12): 308-314.

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Purification and Characterization of Parvalbumin Isotypes from Japanese Flounder (Paralichthys olivaceus)

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