scholarly journals Sequence analysis of the COOH terminus of the alpha-chain of the fourth component of human complement. Identification of the site of its extracellular cleavage.

1986 ◽  
Vol 261 (19) ◽  
pp. 9065-9069
Author(s):  
G Hortin ◽  
A C Chan ◽  
K F Fok ◽  
A W Strauss ◽  
J P Atkinson
Keyword(s):  
Sequence Analysis ◽  
Human Complement ◽  
Alpha Chain ◽  
Fourth Component

scholarly journals The isolation and structure of C4, the fourth component of human complement

1977 ◽  
Vol 165 (3) ◽  
pp. 439-446 ◽  
Author(s):  
I Gigli ◽  
I von Zabern ◽  
R R Porter
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequences ◽  
Human Complement ◽  
Beta Chain ◽  
Terminal Amino Acid ◽  
Gamma Chain ◽  
Alpha Chain ◽  
Terminal Amino ◽  
Alpha Beta ◽  
Fourth Component

The fourth component of complement, C4, was isolated from human serum in good yield, and in confirmation of previous reports was shown to be formed from three peptide chains, alpha, beta and gamma, with apparent mol.wts. 90 000, 80 000 and 30 000 respectively. Preparative methods are described for the isolation of the three peptide chains and their amino acid analyses reported. Component C4 contains 7.0% carbohydrate, alpha-chain 8.6% and the beta-chain 5.6%. The N-terminal amino acid sequences are given for 12 residues of the alpha-chain, eight of the beta-chain and 19 of the gamma-chain.

scholarly journals Variation of gonococcal lipooligosaccharide structure is due to alterations in poly-G tracts in lgt genes encoding glycosyl transferases.

1996 ◽  
Vol 183 (1) ◽  
pp. 323-327 ◽  
Author(s):  
Q L Yang ◽  
E C Gotschlich
Keyword(s):  
Sequence Analysis ◽  
Neisseria Gonorrhoeae ◽  
Experimental Evidence ◽  
High Frequency ◽  
Genetic Mechanism ◽  
Frequency Variation ◽  
Alpha Chain ◽  
Glycosyl Transferases ◽  
Genes Encoding

The lipooligosaccharide (LOS) expressed by gonococci spontaneously varies its structure at high frequency, but the underlying genetic mechanism has not been described. We have previously reported that the genes encoding the glycosyl transferases responsible for the biosynthesis of the variable alpha chain of the LOS of Neisseria gonorrhoeae are located in a locus containing five genes, lgtA, lgtB, lgtC, lgtD, and lgtE. Sequence analysis showed that lgtA, lgtC, and lgtD contained poly-G tracts within the coding frames, leading to the hypothesis that shifts in the number of guanosine residues in the poly-G tracts might be responsible for the high frequency variation in structure of gonococcal LOS. We now provide experimental evidence confirming this hypothesis.

Production of Antibody Against the Fourth Component of Human Complement

Vox Sanguinis ◽  
1964 ◽  
Vol 9 (1) ◽  
pp. 91-95 ◽  
Author(s):  
Margaret J. Polley ◽  
Erna M. Rochna ◽  
P. L. Mollison
Keyword(s):  
Human Complement ◽  
Fourth Component

Formation of Covalent Complexes between the Fourth Component of Human Complement and IgG Immune Aggregates

Complement ◽  
1987 ◽  
Vol 4 (1) ◽  
pp. 21-32 ◽  
Author(s):  
J.M. Alcolea ◽  
L.C. Antón ◽  
G. Marqués ◽  
P. Sánchez-Corral ◽  
F. Vivanco
Keyword(s):  
Human Complement ◽  
Fourth Component ◽  
Immune Aggregates

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
Keyword(s):  
Primary Structure ◽  
Protein Sequence ◽  
Human Complement ◽  
Cdna Sequencing ◽  
Complement C4 ◽  
Fourth Component ◽  
Polypeptide Chains ◽  
Complete Primary Structure

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.

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