STUDIES OF HUMAN FACTOR VIII/ VON WILLEBRAND FACTOR.
Item
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Title
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STUDIES OF HUMAN FACTOR VIII/ VON WILLEBRAND FACTOR.
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Identifier
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AAI8222932
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identifier
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8222932
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Creator
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BOBROW, MARK N.
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Contributor
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Aaron Lukton
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Date
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1982
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Language
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English
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Publisher
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City University of New York.
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Subject
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Chemistry, Biochemistry
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Abstract
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A method was developed to produce a murine antibody in ascitic fluid to human factor VIII/von Willebrand factor. The murine antiserum was comparable to a commercial rabbit antiserum when used to quantitate factor VIII related antigen by immunoelectrophoresis and enzyme immunoassay.;The structure of factor VIII/von Willebrand factor was examined by circular dichroism spectroscopy. F VIII/vWF was found to have approximately 50% unordered or random coil structure and less than 15% (alpha) helical structure. It appears to be a structurally stable protein since changes in its CD spectrum were minimal after heating, and in the pH range 5-9. F VIII/vWF most likely contains many disulfide bonds which are responsible for its stability. This is evident in the change in its CD spectrum on the addition of dithiothreitol.;The interaction between F VIII/vWF and heparin was investigated. F VIII/vWF bound to heparin at physiological pH and ionic strength. By increasing the ionic strength, F VIII/vWF eluted retaining all of its biological activities. From the pH dependence, and the effect of calcium and citrate on the interaction, it appears that it occurs by two independent mechanisms. One is through a positively charged residue on F VIII/vWF and the other involves intrinsic calcium.;The replacement of calcium by terbium was undetectable by fluorescence.
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Type
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dissertation
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Source
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PQT Legacy CUNY.xlsx
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degree
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Ph.D.
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Program
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Biochemistry
