Identification of amino acid residues in cobra venom factor responsible for convertase stability by forming bonds with human factor B

Toxicon ◽  
2020 ◽  
Vol 182 ◽  
pp. S10
Author(s):  
B.E. Hew ◽  
D.C. Fritzinger ◽  
C.-W. Vogel
Toxicon ◽  
2020 ◽  
Vol 184 ◽  
pp. 68-77
Author(s):  
Brian E. Hew ◽  
Michael K. Pangburn ◽  
Carl-Wilhelm Vogel ◽  
David C. Fritzinger

1986 ◽  
Vol 261 (24) ◽  
pp. 11038-11044 ◽  
Author(s):  
P Hensley ◽  
M C O'Keefe ◽  
C J Spangler ◽  
J C Osborne ◽  
C W Vogel

2009 ◽  
Vol 28 (16) ◽  
pp. 2469-2478 ◽  
Author(s):  
Bert J C Janssen ◽  
Lucio Gomes ◽  
Roman I Koning ◽  
Dmitri I Svergun ◽  
Abraham J Koster ◽  
...  

1983 ◽  
Vol 209 (1) ◽  
pp. 51-60 ◽  
Author(s):  
J Gagnon ◽  
D L Christie

The alignment of all the CNBr-cleavage peptides of fragment Bb from human Factor B (a component of the alternative pathway of complement) was determined. This was derived from cleavage of the fragment Bb at arginine residues by using trypsin and clostripain. Details of the isolation and amino acid sequences of these peptides are given. Together with previously published N-terminal sequences of the CNBr-cleavage peptides [Christie & Gagnon (1982) Biochem. J. 201, 555-567], this provides the amino acid sequence of the N-terminal half of fragment Bb.


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