原创力文档sequential extraction results in improved proteome profiling of medicinal plant pinellia ternata tubers, which contain large amounts of high-abundance proteins顺序提取结果提高药用植物的蛋白质组分析半夏ternata块茎,含有大量丰富的蛋白质.pdfVIP
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sequential extraction results in improved proteome profiling of medicinal plant pinellia ternata tubers, which contain large amounts of high-abundance proteins顺序提取结果提高药用植物的蛋白质组分析半夏ternata块茎,含有大量丰富的蛋白质
Sequential Extraction Results in Improved Proteome
Profiling of Medicinal Plant Pinellia ternata Tubers,
Which Contain Large Amounts of High-Abundance
Proteins
XiaoLin Wu., ErHui Xiong., SuFang An, FangPing Gong, Wei Wang*
Key Laboratory of Physiological Ecology and Genetic Improvement of Food Crops in Henan Province, College of Life Science, Henan Agricultural University, Zhengzhou,
China
Abstract
Pinellia ternata tuber is one of the well-known Chinese traditional medicines. In order to understand the pharmacological
properties of tuber proteins, it is necessary to perform proteome analysis of P. ternata tubers. However, a few high-
abundance proteins (HAPs), mainly mannose-binding lectin (agglutinin), exist in aggregates of various sizes in the tubers
and seriously interfere with proteome profiling by two-dimensional electrophoresis (2-DE). Therefore, selective depletion of
these HAPs is a prerequisite for enhanced proteome analysis of P. ternata tubers. Based on differential protein solubility, we
developed a novel protocol involving two sequential extractions for depletion of some HAPs and prefractionation of tuber
proteins prior to 2-DE. The first extraction using 10% acetic acid selectively extracted acid-soluble HAPs and the second
extraction using the SDS-containing buffer extracted remaining acid-insoluble proteins. After application of the protocol, 2-
DE profiles of P. ternata tuber proteins were greatly improved and more protein spots were detected, especially low-
abundance proteins. Moreover, the subunit composition of P. ternata lectin was analyzed by electrophoresis. Native lectin
consists of two hydrogen-bonded subunits (11 kDa and 25 kDa) and the 11 kDa subunit was a glycoprotein. Subsequently,
major HAPs in the tubers were analyzed by mass spectrometry, with nine protein spots being identified as lectin isoforms.
The method
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