Journal article
Identification of the disulfide bonds of human complement C1s.
- Hess D Institute of Biochemistry, University of Bern, Switzerland.
- Schaller J
- Rickli EE
- 1991-03-19
Published in:
- Biochemistry. - 1991
Amino Acid Sequence
Complement C1s
Cystine
Disulfides
Endopeptidases
Humans
Indicators and Reagents
Models, Structural
Molecular Sequence Data
Peptide Fragments
Protein Conformation
English
C1s, one of the three subcomponents of C1, the first component of the complement system, is a complex serine protease. To determine the disulfide-bonding pattern, fragments of C1s were generated by cleavage with pepsin, thermolysin, or subtilisin. Disulfide bonds have been identified by several methods, for example, direct observation of the phenylthiohydantoin derivative of cystine during Edman degradation of isolated peptides and placement in the known cDNA sequence. All of the 26 half-cystines are linked in disulfide bonds occurring at positions 50-68, 120-132, 128-141, 143-156, 160-187, 219-236, 279-326, 306-339, 344-388, 371-406, 410-534, 580-603, and 613-644. All of the disulfide bonds of the earlier described substructures of C1s, the EGF-homologous part, the two SCR units, and the two domains typical for C1s and C1r are localized within these domains.
- Language
-
- English
- Open access status
- closed
- Identifiers
-
- DOI 10.1021/bi00225a014
- PMID 2007122
- Persistent URL
- https://sonar.ch/global/documents/32632
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