Two-dimensional electrophoresis of peptides from human-CHO cell hybrids containing human chromosome 21

1983 ◽  
Vol 9 (6) ◽  
pp. 687-697 ◽  
Author(s):  
C. H. Scoggin ◽  
S. Paul ◽  
Y. E. Miller ◽  
D. Patterson
1981 ◽  
Vol 7 (4) ◽  
pp. 389-398 ◽  
Author(s):  
C. H. Scoggin ◽  
E. Gabrielson ◽  
J. N. Davidson ◽  
C. Jones ◽  
D. Patterson ◽  
...  

1995 ◽  
Vol 21 (6) ◽  
pp. 415-428 ◽  
Author(s):  
Sharon L. Graw ◽  
Katheleen Gardiner ◽  
Karen Hall-Johnson ◽  
Iris Hart ◽  
Anthony Joetham ◽  
...  

1995 ◽  
Vol 21 (5) ◽  
pp. 357-365
Author(s):  
Isik G. Yulug ◽  
Ann M. Killary ◽  
Arbansjit K. Sandhu ◽  
Raghbir S. Athwal ◽  
Margaret Fox ◽  
...  

1984 ◽  
Vol 65 (3) ◽  
pp. 291-294 ◽  
Author(s):  
Flemming Skovby ◽  
Natalie Krassikoff ◽  
Uta Francke

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.


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