Primary Structure of Bovine Plasma High-Molecular-Weight Kininogen. The Amino Acid Sequence of a Glycopeptide Portion (Fragment 1) Following the C-Terminus of the Bradykinin Moiety1

1976 ◽  
Vol 79 (6) ◽  
pp. 1201-1222 ◽  
Author(s):  
Yong Nam HAN ◽  
Hisao KATO ◽  
Sadaaki IWANAGA ◽  
Tomoji SUZUKI
1978 ◽  
Vol 83 (1) ◽  
pp. 213-221 ◽  
Author(s):  
Yong Nam HAN ◽  
Hisao KATO ◽  
Sadaaki IWANAGA ◽  
Sachiko OH-ISHI ◽  
Makoto KATORI

1982 ◽  
Vol 207 (2) ◽  
pp. 253-260 ◽  
Author(s):  
M A Smith ◽  
L M Gerrie ◽  
B Dunbar ◽  
J E Fothergill

Purification of C4a from heat-activated bovine plasma by elution from CM-Sephadex C-50 at pH 7.4 and gel filtration on Sephadex G-50 gives a 20% yield of pure C4a. The complete amino acid sequence of bovine C4a has been determined by automatic sequencer degradation of CNBr and enzymic fragments, and by carboxypeptidase digestion. The 77-residue bovine sequence shows 12 differences from the human sequence with five of these differences occurring in the C-terminal 11 residues. The sequence of C4a confirms earlier suggestions of homology with C3a and C5a: the three sequences show an almost equal number of identities with each other. The six cysteine residues of the ‘disulphide knot’ are conserved as well as seven other residues including the C-terminal arginine.


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