@article{oai:hsuh.repo.nii.ac.jp:00008313,
 author = {Satoko, KITAJO and IEKO, Masahiro and NAITO, Sumiyoshi and NOTOYA, Atsushi and MATSUMOTO, Yoshito and KITAJO, Satoko and IEKO, Masahiro and NAITO, Sumiyoshi and NOTOYA, Atsushi and MATSUMOTO, Yoshito},
 issue = {2},
 journal = {東日本歯学雑誌},
 month = {Dec},
 note = {P(論文), A potent, proteinaceous inducer of coagulation factors, has been purified to homogeneity from Trimeresurus okinavensis (Himehabu snake) by ion exchange chromatography and molecular sieving. It has an apparent molecular weight of 28,000 and it specifically converts fibrinogen to fibrin through an enzymatic reaction. This activity was confirmed by a method using synthetic substrate S-2238, though the fraction from a DEAE sephacel column chromatography shows amidolytic activity of S-2251 and S-2366, which are commonly used to measure plasmin and activated protein C activity, respectively, as well as S-2238. This thrombin-like activity of the final product was not affect by the addition of heparin and AT-III. This enzyme also aggregates normal platelets. It is considered that this purified enzyme would be useful as a hemostatic agent or research reagent.},
 pages = {217--226},
 title = {<ORIGINAL ARTICLE>Characterization of a new coagulant enzyme isolated from Trimeresurus okinavensis (Himehabu snake) venom},
 volume = {16},
 year = {1997}
}