PORCINE WILLEBRAND FACTOR - POPULATION OF MULTIMERS

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  • 1 January 1978
    • journal article
    • research article
    • Vol. 91  (2) , 307-320
Abstract
Purified porcine Willebrand factor was analyzed by agarose-sodium dodecylsulfate electrophoresis. Multiple forms of the protein was found in a series of increasing MW. A molecular mass calibration curve was constructed with fibrinogen (3.4 .times. 105 daltons), Ig[immunoglobulin]M (1 .times. 106 daltons), and glutaraldehyde-crosslinked IgM polymers (2, 3, and 4 .times. 106 daltons). As measured by this procedure, the apparent MW of Willebrand factor polymers ranged from 1.1 .times. 106-2.1 .times. 107. Each member of the series differed from by approximately 1.5 to 1.9 .times. 106 daltons, indicating that members of the series were polymers of 6-mers to 8-mers of the 2.3 .times. 105 dalton subunit. Various purification procedures, used to isolate Willebrand factor active in inducing platelet aggregation, fractionated the polymers, in part, on the basis of size. The same purification procedures, when applied to procine von Willebrand plasma, failed to yield protein of MW greater than 1.1 .times. 106.