Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8334792 | International Journal of Biological Macromolecules | 2012 | 6 Pages |
Abstract
Prolactin inducible protein (PIP) is a 17Â kDa glycoprotein. It binds to many proteins including fibrinogen, actin, keratin, myosin, immunoglobulin G, CD4, and human zinc-alpha-2 glycoprotein. Its ability to bind a large array of proteins indicates its multifaceted role in various biological processes, such as fertility, immunoregulation, antimicrobial activity, apoptosis, and tumor progression. Here, we present the first report of native human serum albumin (HSA)-PIP complex formation in seminal plasma. The complex was purified by chromatographic separation techniques, analyzed by gel electrophoresis, identified by MALDI-TOF mass spectrometry and validated by co-immunoprecipitation coupled with western blotting experiments. Moreover, the behavior of complex in solution was analyzed by dynamic light scattering and interacting residues were identified by in silico protein-protein docking. The purified protein complex shows two bands (67Â kDa and 17Â kDa) on SDS-PAGE gel and a single band (â¼85Â kDa) on native PAGE gel. The predicted complex structure has 13 intermolecular hydrogen bonds, which may contribute to the overall stability of the complex. As HSA has been known to preserve the motility of sperm, native HSA-PIP complex formation may point towards an important role of PIP, which can directly be correlated with male fertility/infertility.
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Authors
Sanjay Kumar, Anil Kumar Tomar, Sudhuman Singh, Mayank Saraswat, Sarman Singh, Tej P. Singh, Savita Yadav,