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pmid: 5080318
Abstract It is shown that Factor X activator of the intrinsic system of blood coagulation consists of a complex of components which can be readily dissociated to their precomplex forms and re-combined to once again produce a Factor X activator. No altered form of Factor VIII or Factor IXa exists which is capable of directly activating Factor X. It is also shown that Factor X activator is most active when both Factors VIII and IXa are complexed to the same phospholipid micelle.
Chromatography, Factor VIII, Phosphatidylethanolamines, Factor VII, In Vitro Techniques, Chromatography, DEAE-Cellulose, Factor IX, Factor X, Chromatography, Gel, Humans, Calcium, Protein Binding
Chromatography, Factor VIII, Phosphatidylethanolamines, Factor VII, In Vitro Techniques, Chromatography, DEAE-Cellulose, Factor IX, Factor X, Chromatography, Gel, Humans, Calcium, Protein Binding
citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 39 | |
popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Average | |
influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 10% | |
impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 10% |