The primary structure of the fourth component of human complement (C4)-C-terminal peptides

1985 ◽  
Vol 5 (10-11) ◽  
pp. 913-921 ◽  
Author(s):  
S. K. Alex Law ◽  
Jean Gagnon

C-terminal CNBr peptides of the three polypeptide chains of C4 were obtained and sequenced. These results supplement previously obtained data, notably the protein sequence derived from cDNA sequencing of pro-C4 (Belt KT, Carroll MC & Porter RR (1984) Cell36, 907–914) and the N-terminal sequences of the three polypeptides (Gigli I, von Zabern I & Porter RR (1977) Biochem. J.165, 439–446), to define the complete primary structure of the plasma form of C4. The β (656 residues), α (748 residues), and γ (291 residues) chains are found in positions 1–656, 661–1408, and 1435–1725 in the pro-C4 molecule.

1983 ◽  
Vol 80 (17) ◽  
pp. 5387-5391 ◽  
Author(s):  
A. S. Whitehead ◽  
G. Goldberger ◽  
D. E. Woods ◽  
A. F. Markham ◽  
H. R. Colten

1974 ◽  
Vol 140 (5) ◽  
pp. 1324-1335 ◽  
Author(s):  
Robert D. Schreiber ◽  
Hans J. Müller-Eberhard

The fourth component of human complement (C4) was shown to be composed of three distinct polypeptide chains linked by disulfide bonds and noncovalent forces. The sum of the molecular weights of the chains equalled that of the intact molecule. The mol wt of the α-, ß-, and γ-chains were respectively, 93,000, 78,000, and 33,000 daltons. Action of C1s on C4 affected only the α-chain, reducing its mol wt to 87,000 daltons. The size of the activation peptide. C4a, is therefore estimated to be 6,000 and that of the major fragment C4b, 198,000 daltons. Periodic acid-Schiff-stained SDS polyacrylamide gels of reduced C4 revealed carbohydrate to be associated with all three chains. A modification of the original method of isolation of C4 is presented.


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