The authors present a clinical description, detailed platelet function analysis, and certain bioc... more The authors present a clinical description, detailed platelet function analysis, and certain biochemical parameters in two siblings with Glanzmann thrombasthenia (G. t.). The isolated occurrence of this disorder in the family corresponds with its autosomal recessive inheritance. In both cases blood platelets completely failed to aggregate. In contrast, the platelet interaction with ristocetin, reflecting their ability to adhere to the subendothelium, the so-called "shape change", the storage granule contents and their release and arachidonic acid metabolism were unaffected. Further, the aggregation abnormality was accompanied by marked procoagulant activity and clot retraction defects; these functions, similarly as aggregation, are implemented on the platelet surface. The analysis of blood platelet proteins, using two dimensional polyacrylamide electrophoresis, confirmed the absence of glycoprotein GP IIb and IIIa and a decrease of the fibrinogen content. The analysis of t...
Journal of chromatography. B, Biomedical applications, Jan 3, 1994
Using Escherichia coli system expressing papilloma virus HPV16 E7MS2 fusion protein as a model sy... more Using Escherichia coli system expressing papilloma virus HPV16 E7MS2 fusion protein as a model system, a novel procedure was applied to solubilize, purify and refold recombinant proteins from E. coli inclusion bodies. The necessity to reactivate proteins at low protein concentrations (owing to their tendency to aggregate at high concentrations) was overcome by solubilization of inclusion bodies in alkaline solution and immobilization of proteins on a strong and resistant anion exchanger. This procedure has an inherent advantage of combining refolding and purification procedures in one step. The solubilization of the fusion protein in an alkaline reagent with the use of an anion exchanger resulted in considerable purification of the recombinant protein at a fairly high concentration. The protein was soluble under mild conditions and reacted with antibodies against the "native" papilloma virus.
The authors present a clinical description, detailed platelet function analysis, and certain bioc... more The authors present a clinical description, detailed platelet function analysis, and certain biochemical parameters in two siblings with Glanzmann thrombasthenia (G. t.). The isolated occurrence of this disorder in the family corresponds with its autosomal recessive inheritance. In both cases blood platelets completely failed to aggregate. In contrast, the platelet interaction with ristocetin, reflecting their ability to adhere to the subendothelium, the so-called "shape change", the storage granule contents and their release and arachidonic acid metabolism were unaffected. Further, the aggregation abnormality was accompanied by marked procoagulant activity and clot retraction defects; these functions, similarly as aggregation, are implemented on the platelet surface. The analysis of blood platelet proteins, using two dimensional polyacrylamide electrophoresis, confirmed the absence of glycoprotein GP IIb and IIIa and a decrease of the fibrinogen content. The analysis of t...
Journal of chromatography. B, Biomedical applications, Jan 3, 1994
Using Escherichia coli system expressing papilloma virus HPV16 E7MS2 fusion protein as a model sy... more Using Escherichia coli system expressing papilloma virus HPV16 E7MS2 fusion protein as a model system, a novel procedure was applied to solubilize, purify and refold recombinant proteins from E. coli inclusion bodies. The necessity to reactivate proteins at low protein concentrations (owing to their tendency to aggregate at high concentrations) was overcome by solubilization of inclusion bodies in alkaline solution and immobilization of proteins on a strong and resistant anion exchanger. This procedure has an inherent advantage of combining refolding and purification procedures in one step. The solubilization of the fusion protein in an alkaline reagent with the use of an anion exchanger resulted in considerable purification of the recombinant protein at a fairly high concentration. The protein was soluble under mild conditions and reacted with antibodies against the "native" papilloma virus.
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Papers by J. Dyr