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
Aoki, Takayoshi
中科院分区:
农林科学1区
文献类型:
--
作者:
Li, Can-Peng;Hayashi, Yoko;Aoki, Takayoshi

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在焦磷酸盐存在下,通过干热使各种蛋白质和糊精磷酸化。和磷酸键的特征。在焦磷酸盐存在下,碱性蛋白质的磷酸化程度高于酸性蛋白质。磷酸化的多聚赖氨酸氢溴酸盐(PP-PLy)和溶菌酶(PP-Lz)比磷酸化的糊精和卵清蛋白(PP-OVA)更容易被磷酸酶脱磷酸化,且PP-PLy的脱磷酸化程度远高于PP-Lz。所有磷酸化样品中的磷酸键在120 ℃加热期间是稳定的。P-31 NMR谱数据表明,PP-PLy中引入了不同类型的磷酸键,其中N-P键是PP-PLy中的主要键。通过质谱分析检测到来自PP-Lz和PP-OVA的一些磷酸化胰蛋白酶肽。此外,在来自PP-Lz和PP-OVA的肽中引入的磷酸酯键被鉴定。(C)2008爱思唯尔有限公司保留所有权利。
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.