BOVINE SEMINAL PLASMA ASFP - LOCALIZATION OF DISULFIDE BRIDGES AND DETECTION OF 3 DIFFERENT ISOELECTRIC FORMS
BOVINE SEMINAL PLASMA ASFP - LOCALIZATION OF DISULFIDE BRIDGES AND DETECTION OF 3 DIFFERENT ISOELECTRIC FORMS
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DOI：
10.1016/0014-5793(94)00362-9
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发表时间：
1994-05-09
期刊：
影响因子：
3.5
通讯作者：
KARG, H
中科院分区：
文献类型：
--
作者：
EINSPANIER, R;KRAUSE, I;KARG, H
酸性精液蛋白 (aSFP) 是从公牛精浆中分离出来的一种主要的 13 kDa 蛋白质，其特征是一种新的生长因子，可刺激体外细胞分裂和卵巢细胞分泌孕激素。在这里，我们确定氧化的 aSFP 的四个半胱氨酸在最近邻残基之间形成两个二硫桥。这种模式在公猪精子粘附素（aSFP 与 aSFP 具有高达 50% 的氨基酸序列同一性）以及最近鉴定的 CUB 结构域家族的其他蛋白质中是保守的。使用等电聚焦结合巯基特异性印迹，aSFP 的三种形式被鉴定为完全氧化（pi 4.7）、部分还原（pi 4.8）和完全还原（pi 5.1）。这些结果表明天然aSFP具有两对不同反应性的半胱氨酸残基。 aSFP 可以保护精子免受氧化损伤的观察结果可能可以通过其还原/氧化行为来解释。
Acidic seminal fluid protein (aSFP) is a major 13 kDa protein isolated from bull seminal plasma and characterized as a new growth factor which stimulates in vitro cell division and progesterone secretion by ovarian cells. Here, we establish that the four cysteines of oxidized aSFP form two disulfide bridges between nearest-neighbour residues. This pattern is conserved in boar spermadhesins, with which aSFP shares up to 50% amino acid sequence identity, and other proteins of the recently identified CUB domain family. Using isoelectric focusing in combination with sulfhydryl group-specific blotting, the three forms of aSFP were identified as completely oxidized (pi 4.7), partly reduced (pi 4.8) and fully reduced at pi 5.1. These results indicate that native aSFP possesses two pairs of cysteine residues of different reactivity. The observation that aSFP can protect sperm from oxidative damage might be explained by its reduction/oxidation behaviour.