@article{oai:niigata-u.repo.nii.ac.jp:00006467,
 author = {Hayashi, Tomohiro and Kamijo, Mikiko and Okushima, Toshimi and Tsuji, Hajime and Masuda, Haruchika and Nakagawa, Katsumi and Nakagawa, Masao and Niiya, Kenji and Sakuragawa, Nobuo},
 issue = {3},
 journal = {Acta medica et biologica, Acta medica et biologica},
 month = {Sep},
 note = {Abnormal antithrombin(AT), designated antithrombin Aomori, is a functionally inactive AT molecule associated with thrombotic disease. Functional analyses of a patient's plasma showed that the antithrombin activity as well as heparin cofactor activity decreased to approximately half of that of control plasma, suggesting that the AT in the patient's plasma contained a variant AT molecule with impaired antithrombin activity. The elution fractions of the patient's plasma from a heparin-Sepharose column showed two major AT peaks. The first peak with obvious antithrombin activity was eluted at a position similar to the control plasma. The second peak with impaired antithrombin activity was eluted at a higher concentration of sodium chloride, indicating that the variant AT has an increased affinity for heparin. Genomic DNA from peripheral white blood cells was prepared for polymerase chain reaction (PCR), and amplified PCR fragments were sequenced. A codon substitution of CGT(Arg^<393>- CAT(His) was observed in the exon 6 of the AT gene, demonstrating a heterozygous Type II AT deficiency with P1 reactive site variant. This patient represents the first case of a reactive site variant of AT in a Japanese family.},
 pages = {157--163},
 title = {Antithrombin Aomori : Identification of a Point Mutation Resulting in Arg^<393> - His Substitution},
 volume = {43},
 year = {1995}
}