Heterozygous Abnormal Fibrinogen Osaka III with the Replacement of γ Arginine-275 by Histidine Has an Apparently Higher Molecular Weight γ-Chain Variant

Nobuhiko Yoshida; Shingi Imaoka; Hajime Hirata; Michio Matsuda; Shinji Asakura

doi:10.1055/s-0038-1646313

Thrombosis and Haemostasis, Inhaltsverzeichnis

Thromb Haemost 1992; 68(05): 534-538
DOI: 10.1055/s-0038-1646313

Original Article

Schattauer GmbH Stuttgart

Heterozygous Abnormal Fibrinogen Osaka III with the Replacement of γ Arginine-275 by Histidine Has an Apparently Higher Molecular Weight γ-Chain Variant

Authors

Nobuhiko Yoshida

¹The institute of Hematology, Jichi Medical School, Tochigi, Japan

²The Department of Internal Medicine, Toshiba General Hospital, Tokyo, Japan
Shingi Imaoka

³The Department of Surgery, the Center for Adult Diseases-Osaka, Osaka, Japan
Hajime Hirata

⁴The Department of Life Science, Faculty of Science, Himeji Institute of Technology, Hyogo, Japan
Michio Matsuda

¹The institute of Hematology, Jichi Medical School, Tochigi, Japan
Shinji Asakura

¹The institute of Hematology, Jichi Medical School, Tochigi, Japan

Abstract

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Summary

Congenitally abnormal fibrinogen Osaka III with the replacement of γ Arg-275 by His was found in a 38-year-old female with no bleeding or thrombotic tendency. Release of fibrinopeptide(s) by thrombin or reptilase was normal, but her thrombin or reptilase time in the absence of calcium was markedly prolonged and the polymerization of preformed fibrin monomer which was prepared by the treatment of fibrinogen with thrombin or reptilase was also markedly defective. Propositus' fibrinogen had normal crosslinking abilities of α- and γ-chains. Analysis of fibrinogen chains on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in the system of Laemmli only revealed the presence of abnormal γ-chain with an apparently higher molecular weight, the presence of which was more clearly detected with SDS-PAGE of fibrin monomer obtained by thrombin treatment. Purified fragment D₁ of fibrinogen Osaka III also seemed to contain an apparently higher molecular weight fragment D₁ γ remnant on Laemmli gels, which was digested faster than the normal control by plasmin in the presence of [ethy-lenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA).

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Referenzen

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