Inhibition of fibrin monomer polymerization by Bence Jones protein in a patient with primary amyloidosis.
The mechanism of inhibition of fibrin monomer polymerization was studied in a patient with primary amyloidosis. Thrombin and reptilase times of the patient's purified fibrinogen (Fbg) were remarkably prolonged, and polymerization of the patient's fibrin monomer was disturbed. Fbg-Bence Jones protein (BJP) complex was demonstrated by immunoelectrophoresis and sodium dodecyl sulfate-polyacrylamide gel electrophoresis on the patient's purified Fbg. The patient's BJP not only prolonged the thrombin time of normal Fbg but also inhibited the polymerization of normal fibrin monomer. These results suggested that in this patient fibrin monomer polymerization was inhibited by binding of BJP to Fbg.
Shigekiyo
T
T
First Department of Internal Medicine, School of Medicine, University of Tokushima, Japan.
Kosaka
M
M
Shintani
Y
Y
Azuma
H
H
Iishi
Y
Y
Saito
S
S
D000368:Aged; D000686:Amyloidosis / Q000097:blood*; D001536:Bence Jones Protein / Q000097:blood*; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D005338:Fibrin Fibrinogen Degradation Products / Q000032:analysis / Q000037:antagonists & inhibitors*; D005340:Fibrinogen / Q000032:analysis / Q000378:metabolism; D006801:Humans; D007122:Immunoelectrophoresis; D010314:Partial Thromboplastin Time; D011517:Prothrombin Time; D013918:Thrombin Time
D005338:Fibrin Fibrinogen Degradation Products; C011468:fibrinmonomer; D005340:Fibrinogen; D001536:Bence Jones Protein