Presence of a serine protease in the complement-activating component of the complement-dependent bactericidal factor, RaRF, in mouse serum.
A 100-kDa protein was isolated from the complement-activating component of mouse Ra-reactive factor. It generated a 29-kDa chain upon reduction. Partial amino acid sequences of the 29-kDa chain were determined after fragmentation with CNBr. A 386-bp-long probe was synthesized by the polymerase chain reaction with oligonucleotide primers designed by reference to the amino acid sequence. Using this probe, we cloned a 3.7-kb DNA from a mouse liver cDNA library. The amino acid sequence of the 29-kDa chain deduced from the nucleotide sequence of this cDNA was consistent with the amino acid sequences determined. The full sequence was found to have characteristics of a serine protease and exhibited 29% and 30% homologies with those of light chains of the C1r and C1s subcomponents of complement, respectively.
Takahashi
A
A
Department of Molecular Biology, School of Medicine, Kitasato University, Kanagawa-ken, Japan.
Takayama
Y
Y
Hatsuse
H
H
Kawakami
M
M
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001770:Blood Bactericidal Activity; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D037601:Mannose-Binding Lectin / Q000031:analogs & derivatives*; D051379:Mice; D008969:Molecular Sequence Data; D016133:Polymerase Chain Reaction; D015183:Restriction Mapping; D016415:Sequence Alignment; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000235:genetics
D002352:Carrier Proteins; D037601:Mannose-Binding Lectin; C445639:Mbl2 protein, mouse; D004247:DNA; D012697:Serine Endopeptidases