大阪鲫两种卵巢蛋白的纯化及其生化特性

Purlfication and Biochemical Characteristics of Two Gonadal Proteins from Carassius auratus Cuvier

应用制备电泳技术，从大阪鲫（ＣａｒａｓｓｉｕｓａｕｒａｔｕｓＣｕｖｉｅｒ）卵匀浆液中提纯两种卵黄蛋白—蛋白质Ｈ及蛋白质Ｌ。蛋白质Ｈ类似卵黄脂磷蛋白（磷为０．２４％，氮为９．１８％，等电点６．７４），分子量４７１０００。在ＳＤＳ电泳中显示４条带，分子量分别为９５８００、９０７００、８６５００、２６９００。蛋白质Ｌ是类卵黄高磷蛋白，其分子量为９４０００。在ＳＤＳ电泳中显示一条带（含磷８．８５％、氰１４．１４％，等电点７．０１），分子量２９４００。同时也观察到在不同ｐＨ值溶液中两种蛋白质紫外光吸收光谱和四阶导数谱变化的现象。

A preparative PAGE was used to purify two yolk proteins: protein H and protein L from homogenates of Carassius auratus Cuvier eggs. Protein H was a lipoprotein (phosphorus=0. 24%, nitrogen= 9. 18%, PI = 6. 74), similar to lipovitellin. Its mol. wt.was 471000, and displayed four bands in SDS-PAGE, corresponding to mol. wt. of 95800,90700, 86500, 26900 respectively. Protein L was a phosphoprotein (phosphorus = 8. 35% ,nitrogen= 14. 14%, PI= 7. 01 ) like phosvitin. But it had different amino acid composition.The mol. wt. of protein L was 94000, and displayed the band in SDS-PAGE,corresponding to mol. wt. of 29400. The change of ultraviolet absorption spectrum and four derivatives spectrum of these two proteins are observed in solutions of different PH values.