Primary structure of guinea-pig Hageman factor: sequence around the cleavage site differs from the human molecule.
The guinea-pig and human Hageman factors differ in their sensitivity to activation by particular bacterial proteinases. To understand this difference, the primary structure and cleavage site on activation of the guinea-pig molecule were determined and compared with the human molecule. By the use of a synthetic oligodeoxyribonucleotide probe which encoded a part of human Hageman factor cDNA, a cDNA clone was isolated from a lambda gt11 cDNA library of guinea-pig liver and sequenced. The cDNA clone was identified as that of guinea-pig Hageman factor by the complete identity of the deduced amino-acid sequence with the actual sequence of the amino-terminal portion of guinea-pig Hageman factor molecule and the active form. The cDNA included part of a leader sequence and the entire coding region of the Hageman factor molecule. Guinea-pig Hageman factor was composed of the same domain structures as the human counterpart with an overall 72% homology in the amino-acid sequence. However, the sequences around the cleavage site were surprisingly different; -Met351-Thr-Arg-Val-Val-Gly-Gly-Leu-Val359-(human) and -Leu338-Ser-Arg-Ile-Val-Gly-Gly-Leu-Val346-(guinea-pig). The amino-acid substitutions around the cleavage site might explain the difference in sensitivity to activation between the human and guinea-pig molecules.
Semba
U
U
Department of Laboratory Medicine, School of Medicine, Kumamoto University, Japan.
Yamamoto
T
T
Kunisada
T
T
Shibuya
Y
Y
Tanase
S
S
Kambara
T
T
Okabe
H
H
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002851:Chromatography, High Pressure Liquid; D004247:DNA; D005174:Factor XII / Q000235:genetics*; D006168:Guinea Pigs; D006801:Humans; D008099:Liver / Q000737:chemistry; D008969:Molecular Sequence Data; D011487:Protein Conformation; D015183:Restriction Mapping
D005174:Factor XII; D004247:DNA