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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

Nobuhiko Yoshida
1   The institute of Hematology, Jichi Medical School, Tochigi, Japan
2   The Department of Internal Medicine, Toshiba General Hospital, Tokyo, Japan
,
Shingi Imaoka
3   The Department of Surgery, the Center for Adult Diseases-Osaka, Osaka, Japan
,
Hajime Hirata
4   The Department of Life Science, Faculty of Science, Himeji Institute of Technology, Hyogo, Japan
,
Michio Matsuda
1   The institute of Hematology, Jichi Medical School, Tochigi, Japan
,
Shinji Asakura
1   The institute of Hematology, Jichi Medical School, Tochigi, Japan
› Author Affiliations
Further Information

Publication History

Received 04 March 1992

Accepted after revision 22 June 1992

Publication Date:
04 July 2018 (online)

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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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