PROTEIN PROFILES OF FLAX GENOTROPHS

1982 ◽  
Vol 24 (4) ◽  
pp. 417-425 ◽  
Author(s):  
Mary Ann Fieldes ◽  
Hugh Tyson ◽  
David Marriott

Protein profiles of partially purified protein extracts from main stem tissue of Durrant's L and S flax (Linum usitatissimum L.) genotrophs were examined with one and two dimensional electrophoresis on acrylamide gels. The purification retained mainly glycoproteins. Among this reduced spectrum of plant proteins, some of the proteins separated had relative mobility (Rm) shifts between L and S. For two proteins, the Rm shifts were demonstrated in two-dimensional separations using mixtures of the L and S extracts. The Rm shifts were all in the same direction, the S protein ran slightly slower than the corresponding L protein, in both dimensions. This shift direction agreed with previous studies on Rm shifts with peroxidase and esterase isozymes and with similar shifts in acid phosphatase isozymes.

1980 ◽  
Vol 22 (4) ◽  
pp. 529-534 ◽  
Author(s):  
H. Tyson ◽  
M. A. Fieldes

Anionic peroxidase isozymes from main stem tissues of adult plants of two flax (Linum usitatissimum L.) genotrophs were separated using acrylamide gel electrophoresis. A range of seven acrylamide concentrations was used for the gels, enabling the effect of gel concentration on relative mobility (Rm) to be examined. The regression of log (Rm) on gel concentration was linear for two of the four main isozymes found. Differences in linear regression slope between the L and S flax genotroph isozymes suggested genotroph differences in molecular weight.


1996 ◽  
Vol 17 (5) ◽  
pp. 855-865 ◽  
Author(s):  
Akira Tsugita ◽  
Masaharu Kamo ◽  
Takao Kawakami ◽  
Yuta Ohki

1982 ◽  
Vol 47 (01) ◽  
pp. 019-021 ◽  
Author(s):  
Cemal Kuyas ◽  
André Haeberli ◽  
P Werner Straub

SummaryHuman fibrinogen was compared with asialofibrinogen by two-dimensional electrophoresis to evaluate the contribution of sialic acid to the heterogeneity of the γ- and Bβ-polypeptide chains.Reduced fibrinogen showed three major variants for both the γ- and Bβ-chains. In addition two minor γ-bands with a more acidic isoelectric point than the normal γ-chains were observed. Electrophoresis in the second dimension (SDS) suggests that these most acidic bands are γ-chain-variants with a higher molecular weight. In asialofibrinogen only two predominant variants with more alkaline isoelectric points were present in each chain type.It is concluded that enzymatic removal of sialic acid partially reduces the heterogeneity of the γ- and Bβ-polypeptide chains of human fibrinogen, but additional sources producing charge heterogeneity must be sought.


2012 ◽  
Vol 18 (5) ◽  
pp. 819 ◽  
Author(s):  
Yanhua YANG ◽  
Weitong CUI ◽  
Xiaoyong LIU ◽  
Keming ZHU ◽  
Keping CHEN

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