[Purification and biochemical characterization of high-molecular-weight-glutenin subunits 14 and 15].Yi Chuan Xue Bao. 2001; 28(1):46-51.YC
Abstract
The high molecular weight glutenin subunits 14 and 15 were purified from cultivars of bread wheat (Triticum aestivum) Xiaoyan 6 by preparative sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) appled a new method for visualizing protein in gels. N-terminal amino acid sequences were homologous comparing with other High-Molecular-Weight glutenin subunits. The result suggested that they were basic protein analyzed by two-dimensional electrophoresis of IEF(Isoelectric Focussing) x SDS-PAGE and NEPHGE(Non-Equilibrium PI-gradient Electrophoresis) x SDS-PAGE.
MeSH
Pub Type(s)
Journal Article
Research Support, Non-U.S. Gov't
Language
chi
PubMed ID
11209711
Citation
Deng, Z Y., et al. "[Purification and Biochemical Characterization of High-molecular-weight-glutenin Subunits 14 and 15]." Yi Chuan Xue Bao = Acta Genetica Sinica, vol. 28, no. 1, 2001, pp. 46-51.
Deng ZY, Zhao HX, Fan SH, et al. [Purification and biochemical characterization of high-molecular-weight-glutenin subunits 14 and 15]. Yi Chuan Xue Bao. 2001;28(1):46-51.
Deng, Z. Y., Zhao, H. X., Fan, S. H., Ji, W. Q., Guo, A. G., & Xue, X. Z. (2001). [Purification and biochemical characterization of high-molecular-weight-glutenin subunits 14 and 15]. Yi Chuan Xue Bao = Acta Genetica Sinica, 28(1), 46-51.
Deng ZY, et al. [Purification and Biochemical Characterization of High-molecular-weight-glutenin Subunits 14 and 15]. Yi Chuan Xue Bao. 2001;28(1):46-51. PubMed PMID: 11209711.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR
T1 - [Purification and biochemical characterization of high-molecular-weight-glutenin subunits 14 and 15].
AU - Deng,Z Y,
AU - Zhao,H X,
AU - Fan,S H,
AU - Ji,W Q,
AU - Guo,A G,
AU - Xue,X Z,
PY - 2001/2/24/pubmed
PY - 2001/3/17/medline
PY - 2001/2/24/entrez
SP - 46
EP - 51
JF - Yi chuan xue bao = Acta genetica Sinica
JO - Yi Chuan Xue Bao
VL - 28
IS - 1
N2 - The high molecular weight glutenin subunits 14 and 15 were purified from cultivars of bread wheat (Triticum aestivum) Xiaoyan 6 by preparative sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) appled a new method for visualizing protein in gels. N-terminal amino acid sequences were homologous comparing with other High-Molecular-Weight glutenin subunits. The result suggested that they were basic protein analyzed by two-dimensional electrophoresis of IEF(Isoelectric Focussing) x SDS-PAGE and NEPHGE(Non-Equilibrium PI-gradient Electrophoresis) x SDS-PAGE.
SN - 0379-4172
UR - https://www.unboundmedicine.com/medline/citation/11209711/[Purification_and_biochemical_characterization_of_high_molecular_weight_glutenin_subunits_14_and_15]_
DB - PRIME
DP - Unbound Medicine
ER -