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PMID: 6981411 Published · ppublish English Journal Article

Completion of the amino acid sequences of the A and B chains of subcomponent C1q of the first component of human complement.

The Biochemical journal ·Vol. 203 ·No. 3 ·1982-06-01 ·Pages 559-69

Reid KB, Gagnon J, Frampton J

Abstract

The sequences of amino acid residues 109--224 of the A chain, and residues 109--22 of the B chain, of human subcomponent C1q are given. These results, along with previously published sequence data on the N-terminal, collagen-like, regions of the A and B chains [Reid (1979) Biochem. J. 179, 367--371] yield the complete amino acid sequences of the A and B chains of subcomponent C1q. The asparagine residue at position A-124 has been identified as the major site of asparagine-linked carbohydrate in subcomponent C1q. When the sequences of the C-terminal, 135-residue-long, 'globular' regions of A and B chains are compared they show 40% homology. The degree of homology over certain stretches of 15--20 residues, within the C-terminal regions, rises up to values of 73%, indicating the presence of strongly conserved structures. Structure prediction studies indicate that both the A and B chain C-terminal regions may adopt a predominantly beta-type structure with apparently little alpha-helical structure.

MeSH Terms
Amino Acid Sequence Amino Acids/analysis Asparagine/analysis Carbohydrates/analysis Complement Activating Enzymes Complement C1q Humans Peptide Fragments/isolation & purification
Chemicals
Amino Acids Carbohydrates Peptide Fragments Asparagine Complement C1q Complement Activating Enzymes
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Reid K B
Gagnon J
Frampton J
References (35)
35 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2030559
Published
1982-06-01
Pages
559-69
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1158269
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2030559 PMC Full Text View journal details
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