Degradation of yolk proteins in sea urchin eggs and embryos

Yukio Yokota , Koichi H. Kato
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引用次数: 63

Abstract

Yolk granules isolated from unfertilized and fertilized eggs of the sea urchins, Hemicentrotus pulcherrimus and Anthocidaris crassispina, were incubated in acidic media, and the protein components were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By the incubation, a protein (molecular weight 180 000 in H. pulcherrimus and 178 000 in A. crassispina) most abundant in unfertilized eggs decreased, while proteins (molecular weight 61 000, 72 000, 94 000, 114 000 in H. pulcherrimus and 56 000, 70 000, 92 000, 112 000 in A. crassispina) dominant in developed embryos increased. Neither alkaline nor neutral condition resulted in such changes in the electrophoretic patterns of proteins as observed in acidic media. Experiments with various inhibitors of proteases suggested that thiol protease(s), such as cathepsin B, may be the most important enzyme(s) in the degradation of yolk proteins in embryogenesis of the sea urchin.

海胆卵和胚胎中卵黄蛋白的降解
将海胆(hemicentrrotus pulcherrimus)和棘海胆(Anthocidaris crassispina)未受精卵和受精卵中分离的卵黄颗粒在酸性培养基中孵育,采用十二烷基硫酸钠-聚丙烯酰胺凝胶电泳法对其蛋白质成分进行分析。经孵育,未受精卵中最丰富的蛋白(H. pulcherrimus分子量为18 000,a . crassispina分子量为17.8 000)减少,而发育胚中优势蛋白(H. pulcherrimus分子量为61 000,72 000,94 000,114 000,a . crassispina分子量为56 000,7 000,92 000,112 000)增加。无论是碱性条件还是中性条件都不会导致在酸性介质中观察到的蛋白质电泳模式的变化。多种蛋白酶抑制剂的实验表明,巯基蛋白酶(如组织蛋白酶B)可能是海胆胚胎发生过程中蛋黄蛋白降解最重要的酶。
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