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1.
Vnitr Lek ; 55(11): I-XII, 2009 Nov.
Article in Czech | MEDLINE | ID: mdl-20017445

ABSTRACT

The registry of patients treated with Thromboreductin (anagrelide) in the Czech Republic contains data concerning patients that have been treated using this drug since 2004. As of June 2009, the total number of patients was 549. The current analysis focused mainly on evaluation of anagrelide dosage needed to achieve a complete response in high-risk patients: reduction in platelet count to below 400 x 10(9)/l, which was also considered as reaching the therapeutic goal. The outcomes of the registry confirm that although anagrelide (Thromboreductin) is a very effective platelet-reducing agent, the administration of which is related to a low incidence of adverse effects and complications, the therapeutic goal is not achieved in all cases and or despite a quick treatment response, the therapeutic goal is achieved more slowly.


Subject(s)
Myeloproliferative Disorders/complications , Platelet Aggregation Inhibitors/therapeutic use , Quinazolines/therapeutic use , Thrombocythemia, Essential/drug therapy , Thrombocytosis/drug therapy , Adult , Aged , Aged, 80 and over , Female , Humans , Male , Middle Aged , Thrombocytosis/complications
2.
Article in English | MEDLINE | ID: mdl-12401348

ABSTRACT

The interaction of bull seminal plasma proteins and sperm with mannan was investigated using an enzyme-linked binding assay (ELBA). A high mannan-binding activity was found in the protein fraction interacting with heparin. Mannan binding to seminal plasma proteins was inhibited by D-mannose and D-fructose, but not by D-mannose-6-phosphate, D-glucose-6-phosphate, ovalbumin and ovomucoid. Mannan inhibited the binding of bovine zona pellucida glycoproteins both to bull sperm and seminal plasma proteins. Yeast mannan immobilized to divinyl sulfone-activated Sepharose was used for the isolation of mannan-binding proteins. The protein components of this fraction were identified on the basis of relative molecular mass determination and N-terminal amino acid sequencing: RNAase dimer, PDC-109 and a protein homologous to BSP-30K (relative molecular mass 14,500). The isolated proteins were characterized by a high zona pellucida binding activity.


Subject(s)
Chromatography, Affinity/methods , Proteins/isolation & purification , Semen/chemistry , Amino Acid Sequence , Animals , Cattle , Electrophoresis, Polyacrylamide Gel , Male , Mannans/chemistry , Proteins/chemistry , Sepharose/chemistry
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