Characterization of the 1B-type ω-gliadins from Triticum aestivum cultivar Butte

被引：71

作者：

DuPont, FM ^{[1
]}

Vensel, WH ^{[1
]}

Chan, R ^{[1
]}

Kasarda, DD ^{[1
]}

机构：

[1] ARS, USDA, Western Reg Res Ctr, Albany, CA 94710 USA

来源：

CEREAL CHEMISTRY | 2000年 / 77卷 / 05期

关键词：

D O I：

10.1094/CCHEM.2000.77.5.607

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

omega-Gliadins were purified from wheat (Triticum aestivum L. 'Butte') flour and characterized. Although reversed-phase HPLC (RP-HPLC) separated the 1B-encoded omega-gliadins into two fractions, 1B1 and 1B2, these fractions had nearly identical amino acid compositions, three similar protein bands in SDS-PAGE, 10 similar spots in two-dimensional PAGE, and two similar N-terminal amino acid sequences. The main components had a range in mass of 48,900-51,500 when estimated by mass spectrometry, significantly less than the mass estimated by SDS-PAGE. The 1B fractions were digested with thermolysin, the peptides were separated by RP-HPLC, the peptide mass was determined, and nine peptides from each fraction were sequenced with nearly identical results for the 1B1 and 1B2 digests. A possible consensus sequence of the 1B-encoded omega-gliadin internal repeat was QQQXP, where X was F, I, or L in descending order of occurrence. The 1D-encoded omega-gliadins were purified by RP-HPLC as a single fraction that had one band in SDS-PAGE, two spots in two-dimensional PAGE, two components with mass of 41,923 and 42,770 detected by mass spectrometry, and two N-terminal sequences. Circular dichroism (CD) spectra for the 1B and 1D omega-gliadins were similar and were suggestive of mainly flexible random structure with a significant amount of the left-handed polyproline II helical conformation in the 1D components.

引用

页码：607 / 614

页数：8

共 40 条

[1] Quantification of individual low-molecular-weight glutenin subunit transcripts in developing wheat grains by competitive RT-PCR [J].