Phosphorylated serine clusters of phosvitin plays a crucial role in the regulatory mineralization
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Updated: Feb 11, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination
Published on: May 18, 2017
Xiaowei Zhang1, Xi Huang2, Meihu Ma2
1State Key Laboratory of Food Nutrition and Safety, Key Laboratory of Food Nutrition and Safety, Ministry of Education of China, College of Food Engineering and Biotechnology, Tianjin University of Science &Technology, Tianjin 300457, China; National R&D Center for Egg Processing, College of Food Science and Technology, Huazhong Agricultural University, Wuhan, Hubei 430070, China.
Abstract:
Phosphorylation of phosvitin has been proved to play an important role in the mineralization, but the active region of phosvitin is still not known yet. Four phosvitin phosphopeptides (PPPs) were obtained after separating from ion exchange column and desalting from gel filtration, and named as PPP0, PPP1, PPP3 and PPP4, respectively. The effect of PPP on the mineralization was investigated by pH-stat system, Fourier transform infrared spectroscopy, X-ray diffraction and scanning electron microscope. SDS-PAGE and circular dichroism were applied to study the composition and the structure of PPP. Results showed that the order of promoting mineralization was as follows: PPP3 > phosvitin > PPP4 > PPP1 > control > PPP0. PPP0 and PPP1 was not involved in the mineralization, while the structure of PPP4 was too compact to promote mineralization because of its high β-sheet conformation. PPP3, which contained a 10 kDa peptide, is the most effective promoter for mineralization. LTQ-MS/MS results indicated that the phosphorylated serine clusters of phosvitin was the active region for promoting mineralization.
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