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Multimerin: a series of large disulfide-linked multimeric proteins within
platelets
CP Hayward, TE Warkentin, P Horsewood and JG Kelton
Department of Medicine, McMaster University Medical Centre, Hamilton,
Ontario, Canada.
Platelets contain proteins with biochemical properties that are well
adapted to promoting hemostasis. One important adhesive protein is von
Willebrand factor (vWF), which is a very large protein comprised of a
series of multimers, ranging from 860,000 to over 10 million daltons. In
this report we describe a second platelet protein, p-155, which has a
similar unique multimeric composition. Using agarose-acrylamide gel
electrophoresis, platelet p-155 was shown to be composed of multimers
ranging from less than 450 Kd to many million daltons. Based on this unique
structure, we propose that the native molecule be designated as multimerin.
Comparison with vWF showed that multimerin contained less of the very high
molecular weight multimers. Differential reduction demonstrated that the
smallest multimer is a trimer, composed of three 155-Kd subunits. Platelet
releasate was demonstrated to contain mainly the smaller multimers,
suggesting that the larger multimers bind to the platelet surface. Other
studies indicate that multimerin and vWF are the two largest platelet
proteins and the only two platelet proteins exhibiting a complex,
disulfide-linked multimeric composition with variability in multimer size.
Volume 77,
Issue 12,
pp. 2556-2560,
06/15/1991
Copyright © 1991 by The American Society of Hematology

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