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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Harrison, R. L. Mckee, P. A. Erickson, H. P. Ohmori, K. Fretto, L. J. Switzer, M. E. |
| Abstract | The structure of native and progressively reduced human factor VIII/von Willebrand factor (FVIII/vWF) was examined by electron microscopy and SDS gel electrophoresis and then correlated with its biological activities. Highly resolved electron micrographs of well-spaced, rotary- shadowed FVIII/vWF molecules showed their structure to consist of a very flexible filament that contains irregularly spaced small nodules. Filaments ranged from 50 to 1,150 nm with a mean length of 478 nm and lacked fixed, large globular domains as seen in fibrinogen and IgM. A population of multimeric FVIII/vWF species ranging in molecular weight from 1 to 5 million daltons and differing in size alternately by one and two subunits was observed on SDS-2% polyacrylamide-0.5% agarose gel electrophoresis. With progressive reduction of disulfide bonds by dithiothreitol (DTT), the electron microscopic size of FVIII/vWF decreased in parallel with increased electrophoretic mobility on SDS- agarose gels; between 0.1 and 0.5 mM DTT its structure changed from predominantly fibrillar species to large nodular forms. A 50% loss of vWF specific activity and FVIII procoagulant activity occurred at 0.4 mM DTT and 1 mM DTT, respectively, corresponding to the reduction of 4 and 12 disulfide bonds of the 62 disulfides per 200,000-dalton subunit. We conclude that reduction of a few critical disulfide bonds results in a major structural change by electron microscopy and a concomitant loss of approximately 50% of the vWF function. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Part | Pt 1 |
| Issue Number | 2 |
| Volume Number | 95 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 1982-11-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Blood Coagulation Factors Dithiothreitol Pharmacology Factor VIII Von Willebrand Factor Alkylation Physiology Blood Platelets Metabolism Macromolecular Substances Mercaptoethanol Microscopy, Electron Molecular Weight Platelet Aggregation Protein Conformation Ristocetin Structure-Activity Relationship Research Support, U.S. Gov't, P.H.S. Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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