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Sökning: WFRF:(Dahlbäck Björn) > (1990-1994) > Bovine C4b binding ...

Bovine C4b binding protein. Molecular cloning of the alpha- and beta-chains provides structural background for lack of complex formation with protein S

Hillarp, Andreas (författare)
Lund University,Lunds universitet,Klinisk kemi, Malmö,Forskargrupper vid Lunds universitet,Clinical Chemistry, Malmö,Lund University Research Groups,Skåne University Hospital
Thern, Anette (författare)
Lund University,Lunds universitet,Avdelningen för medicinsk mikrobiologi,Institutionen för laboratoriemedicin,Medicinska fakulteten,Division of Medical Microbiology,Department of Laboratory Medicine,Faculty of Medicine,Skåne University Hospital
Dahlbäck, Björn (författare)
Lund University,Lunds universitet,Klinisk kemi, Malmö,Forskargrupper vid Lunds universitet,Clinical Chemistry, Malmö,Lund University Research Groups,Skåne University Hospital
 (creator_code:org_t)
1994
1994
Engelska.
Ingår i: Journal of immunology. - 0022-1767. ; 153:9, s. 4190-4199
  • Tidskriftsartikel (refereegranskat)
Abstract Ämnesord
Stäng  
  • C4b binding protein (C4BP) regulates the complement system. It also interacts with anticoagulant protein S and with serum amyloid P component. Human C4BP is composed of seven identical 70-kDa alpha-chains and one 45-kDa beta-chain. The binding site for C4b is located on the alpha-chain, whereas the beta-chain binds protein S. Nothing is known about the structure and function of bovine C4BP. No complexed form of protein S was detected by using a gel filtration chromatography system combined with Western blotting. Bovine cDNA clones encoding the C4BP alpha- and beta-chains were isolated from a bovine liver cDNA library. Three overlapping alpha-chain clones predicted a 562-amino acid residues-long mature polypeptide. The overall amino acid sequence similarity with the human alpha-chain was 61%. Like its human counterpart, the bovine alpha-chain is composed of eight contiguous short consensus repeat units, each of approximately 60 amino acid residues, and a carboxyl-terminal nonrepeat region. One bovine beta-chain clone was found and characterized. It predicted a mature bovine beta-chain of 181 amino acid residues. The identity with the human beta-chain was 65% at the amino acid level. A noteworthy difference between bovine and human beta-chains was that the bovine beta-chain only contained two short consensus repeats compared with three in human beta-chain. Sequence alignment indicates that the region corresponding to residues 1-60 (repeat 1) in the human beta-chain is absent in the homologous bovine polypeptide. Because the short consensus repeats of the human beta-chain contain the binding site for protein S, the lack of one repeat unit in the bovine beta-chain may provide a clue to the lack of complex formation between C4BP and protein S in bovine plasma.

Ämnesord

MEDICIN OCH HÄLSOVETENSKAP  -- Medicinska och farmaceutiska grundvetenskaper -- Mikrobiologi inom det medicinska området (hsv//swe)
MEDICAL AND HEALTH SCIENCES  -- Basic Medicine -- Microbiology in the medical area (hsv//eng)

Nyckelord

Amino Acid Sequence
Animals
Base Sequence
Blotting, Western
Carrier Proteins/chemistry
Cattle
Chromatography, Gel
Cloning, Molecular
Humans
Integrin alphaXbeta2
Molecular Sequence Data
Polymerase Chain Reaction
Protein Binding
Protein S/metabolism
Sequence Homology, Amino Acid

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Av författaren/redakt...
Hillarp, Andreas
Thern, Anette
Dahlbäck, Björn
Om ämnet
MEDICIN OCH HÄLSOVETENSKAP
MEDICIN OCH HÄLS ...
och Medicinska och f ...
och Mikrobiologi ino ...
Artiklar i publikationen
Journal of immun ...
Av lärosätet
Lunds universitet

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