Department of Biophysics, All India Institute of Medical Sciences, New Delhi, India.
Int J Biol Macromol. 2013 Jan;52:296-9. doi: 10.1016/j.ijbiomac.2012.10.011. Epub 2012 Oct 22.
Identification of protein-protein interactions is vital for complete understanding of a biological process and for functional characterization of a protein in related biochemical pathways. In this study, we performed analysis of prolactin inducible protein (PIP) interactions in human seminal plasma. PIP and its interacting partners were co-immunoprecipitated, analyzed by SDS-PAGE and identified by MALDI-TOF mass spectrometry. Three major interacting partners were identified, viz. human serum albumin, zinc-α-2 glycoprotein and semenogelin I fragments. This is the first report of interaction between PIP and semenogelin I fragments in human seminal plasma or elsewhere with a suggestive role in reproductive physiology which might be helpful for spermatozoa to acquire their motility.
鉴定蛋白质-蛋白质相互作用对于全面了解生物过程和相关生化途径中蛋白质的功能特征至关重要。在这项研究中，我们对人精液中的催乳素诱导蛋白（PIP）相互作用进行了分析。PIP 及其相互作用的伴侣通过共免疫沉淀被捕获，然后通过 SDS-PAGE 进行分析，并通过 MALDI-TOF 质谱进行鉴定。鉴定出了三个主要的相互作用伴侣，即人血清白蛋白、锌-α-2 糖蛋白和精核蛋白 I 片段。这是 PIP 与精液蛋白 I 片段在人精液或其他地方相互作用的首次报道，这可能对精子获得运动能力具有提示作用，从而有助于生殖生理学。
