Phosphorylation of proteins by dry-heating in the presence of pyrophosphate and some characteristics of introduced phosphate groups
Phosphorylation of proteins by dry-heating in the presence of pyrophosphate and some characteristics of introduced phosphate groups
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DOI:
10.1016/j.foodchem.2008.10.066
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发表时间:
2009-06-01
期刊:
影响因子:
8.8
通讯作者:
Aoki, Takayoshi
中科院分区:
文献类型:
--
作者:
Li, Can-Peng;Hayashi, Yoko;Aoki, Takayoshi
Various proteins and dextrin were phosphorylated by dry-heating in the presence of pyrophosphate. and phosphate bonds characterised. The basic proteins were more highly phosphorylated than acidic proteins by dry-heating in the presence of pyrophosphate. The phosphorylated poly-L-lysine hydrobromide (PP-PLy) and lysozyme (PP-Lz) were more highly dephosphorylated than phosphorylated dextrin and ovalbumin (PP-OVA) by phosphatases, and the dephosphorylation of PP-PLy was much higher than that of PP-Lz. The phosphate bonds in all phosphorylated samples were stable during heating at 120 degrees C. The P-31 NMR spectral data suggested that different types of phosphate bonds were introduced, and the N-P bond was suggested in PP-PLy. Some phosphorylated tryptic peptides from PP-Lz and PP-OVA were detected by mass spectrometry analysis. Furthermore, the introduced phosphate linkages in peptides from PP-Lz and PP-OVA were identified. (C) 2008 Elsevier Ltd. All rights reserved.