Characterization of human blood platelet membrane proteins and glycoproteins by their isoelectric point (pI) and apparent molecular weight using two-dimensional electrophoresis and surface-labelling techniques

1980 ◽  
Vol 599 (2) ◽  
pp. 473-483 ◽  
Author(s):  
John L. McGregor ◽  
Kenneth J. Clemetson ◽  
Elizabeth James ◽  
Ernst F. Luscher ◽  
Marc Dechavanne

Author(s):  
Philip W. Pemberton ◽  
Robert W. Lobley ◽  
Raymond Holmes ◽  
Susanne H. Sørensen ◽  
Kenneth W. Simpson ◽  
...  




2017 ◽  
Vol 13 (1) ◽  
pp. 63-68
Author(s):  
Artūras Serackis ◽  
Dalius Matuzevičius ◽  
Dalius Navakauskas ◽  
Eldar Šabanovič ◽  
Andrius Katkevičius ◽  
...  

Abstract The aim of the investigation presented in this paper was to develop a software-based assistant for the protein analysis workflow. The prior characterization of the unknown protein in two-dimensional electrophoresis gel images is performed according to the molecular weight and isoelectric point of each protein spot estimated from the gel image before further sequence analysis by mass spectrometry. The paper presents a method for automatic and robust identification of the protein standard band in a two-dimensional gel image. In addition, the method introduces the identification of the positions of the markers, prepared by using pre-selected proteins with known molecular mass. The robustness of the method was achieved by using special validation rules in the proposed original algorithms. In addition, a self-organizing map-based decision support algorithm is proposed, which takes Gabor coefficients as image features and searches for the differences in preselected vertical image bars. The experimental investigation proved the good performance of the new algorithms included into the proposed method. The detection of the protein standard markers works without modification of algorithm parameters on two-dimensional gel images obtained by using different staining and destaining procedures, which results in different average levels of intensity in the images.



1997 ◽  
Vol 18 (15) ◽  
pp. 2823-2831 ◽  
Author(s):  
Christian Scheler ◽  
Eva-Christina Müller ◽  
Joachim Stahl ◽  
Ursula Müller-Werdan ◽  
Johann Salnikow ◽  
...  






1986 ◽  
Vol 28 (1) ◽  
pp. 76-83 ◽  
Author(s):  
P. R. Shewry ◽  
S. Parmar ◽  
N. Fulrath ◽  
D. D. Kasarda ◽  
T. E. Miller

The chromosomal locations of the structural genes for secalin storage proteins in Secale cereale and S. montanum were determined by electrophoresis of grain proteins from wheat–rye addition and substitution lines. The use of several different extraction procedures and high-resolution electrophoretic systems (one and two dimensional) enabled us to demonstrate that the genes for all the high molecular weight secalins are present on chromosome IRL, and for all the ω-secalins and at least some of the γ-secalins with a relative molecular mass (Mr) of 40 000 on chromosome IRS of both species. In contrast, the genes for the γ-secalins (Mr = 75 000) are located on 2RcS in S. cereale but 6Rm in S. montanum. These observations are discussed in relation to evolution of prolamins and their genes in Secale and related members of the Triticeae.Key words: Secale, rye, seed proteins, structural genes, two-dimensional electrophoresis.



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