Proteins of the vitelline membrane of quail (Coturnix coturnix japonica) eggs.

Proteins of the vitelline membrane of quail (Coturnix coturnix japonica) eggs.
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鹌鹑蛋卵黄膜的蛋白质。

DOI:
10.3382/ps.0721566
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发表时间:
1993
期刊:
影响因子:
4.4
通讯作者:
N. Masuda
N. Masuda
中科院分区:
农林科学2区
文献类型:
--
作者:
M. Mori;N. Masuda

文献摘要

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采用SDS-PAGE对鹌鹑卵卵黄膜蛋白进行了分析。10个主要条带,分子量范围从14.5至285 kDa,可以清楚地区分。在膜内层检测到对应于33和175 kDa分子量的两条带,两者均用过碘酸-希夫试剂染色,表明它们是糖蛋白。在膜的外层检测到9条带。其中,265-和285-kDa的带是糖蛋白。鸡蛋在25 ℃贮藏期间,蛋黄指数显著下降.在卵黄膜的10种蛋白质中,20-kDa蛋白质的减少是最突出的,在储存5天后消失。16.5-和175-kDa的蛋白质条带也不太突出,而40-和61-kDa的蛋白质在储存过程中增加。这些卵黄膜蛋白质的变化也在4 ℃下储存的卵中观察到,尽管变化发生得比25 ℃下储存的卵慢。
Proteins in the vitelline membrane of quail (Coturnix coturnix japonica) eggs were analyzed by SDS-PAGE. Ten major bands, molecular mass ranging from 14.5 to 285 kDa, can be clearly distinguished. Two bands corresponding to the molecular masses of 33 and 175 kDa were detected in the inner layer of the membrane and both were stained with periodic acid-Schiff reagent, indicating that they are glycoproteins. Nine bands were detected in the outer layer of the membrane. Among them, 265- and 285-kDa bands were glycoproteins. During storage of eggs at 25 C, the yolk index significantly decreased. Among the 10 proteins of the vitelline membrane, a decrease in the 20-kDa protein was most prominent, disappearing after 5 days of storage. The 16.5- and 175-kDa protein bands were also less prominent, whereas the 40- and 61-kDa proteins increased during storage. These changes in the proteins of the vitelline membrane were also observed in eggs stored at 4 C, although the changes occurred more slowly than that noted from the eggs stored at 25 C.