Abstract:
:An inhibitor of blood coagulation, a new protein with an apparent molecular weight of 34,000 and an isoelectric point of 4.9, was purified from human placental tissue by EDTA extraction. Five cDNA clones were isolated from the human placental lambda gt11 cDNA library using the mouse monoclonal antibody raised against the coagulation inhibitor as the probe. The longest insert consists of 1,566 nucleotides, and contains 960 nucleotides entirely encoding the 320 amino acids of the inhibitor, and a poly A tail. The deduced amino acid sequence was corroborated by chemical analyses of the protein. The entire amino acid sequence shows homology to those of lipocortin I, lipocortin II, and endonexin-related proteins. The cDNA for the inhibitor was expressed in Escherichia coli under the regulation of the trc promotor of the plasmid pKK233-2. The resulting recombinant protein manifested inhibitory activities against both blood coagulation and phospholipase A2 activity, as did the coagulation inhibitor isolated from human placenta.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Iwasaki A,Suda M,Nakao H,Nagoya T,Saino Y,Arai K,Mizoguchi T,Sato F,Yoshizaki H,Hirata Mdoi
10.1093/oxfordjournals.jbchem.a122165subject
Has Abstract,Author List Incompletepub_date
1987-11-01 00:00:00pages
1261-73issue
5eissn
0021-924Xissn
1756-2651journal_volume
102pub_type
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