Electrofocusing and two-dimensional electrophoresis of bovine caseins

1981 ◽  
Vol 48 (2) ◽  
pp. 303-310 ◽  
Author(s):  
Patrick Trieu-Cuot ◽  
Jean-Claude Gripon

SummaryThe main components of bovine whole casein were characterized by electrofocusing; pi values of αs1-, β-, κ-, γ1-, γ2- and γ3-caseins were determined. A further identification of casein components was achieved by a 2-dimensional electrophoresis study. 2-Dimensional patterns of γ-caseins obtained from a hydrolysate of β-cascin by bovine plasmin are in good agreement with those of γ-caseins naturally present in whole casein.

1992 ◽  
Vol 284 (3) ◽  
pp. 813-817
Author(s):  
C Laurent-Winter ◽  
I Dugail ◽  
A Quignard-Boulange ◽  
X Le Liepvre ◽  
M Lavau

Using two-dimensional electrophoresis on total extracts of adipose tissue from young lean (Fa/fa) and obese (fa/fa) Zucker rats, we have investigated the existence of early events at the protein level, before obvious obesity. Our results indicate that the two genotypes do not differ at 3 days of age in terms of polypeptide pattern. By 7 days of age, two polypeptides are transiently repressed in the fatty genotype, leading us to suggest their potential involvement in the onset of obesity. However, most of the differences between the lean and obese rats are detected at 30 days of age, characterized by an increase in the accumulation of several peptides in the adipose tissue of obese rats, in good agreement with the multiple biochemical changes previously identified at this stage of the disease. These results present evidence of new peptides that may be of interest in the study of the obesity syndrome.


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

Sign in / Sign up

Export Citation Format

Share Document