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1.
Arch Virol ; 150(2): 247-59, 2005 Feb.
Article in English | MEDLINE | ID: mdl-15480855

ABSTRACT

Hepatitis B surface antigen, when produced in yeast (rHBsAg), is capable of binding to cells that express the lipopolysaccharide coreceptor CD14. This interaction is enhanced by a serum protein, the lipopolysaccharide binding protein (LBP). Here we report that most of the rHBsAg particles that attached to monocytes at 0 degrees C, were not endocytosed but were released back into the serum-containing binding buffer at 37 degrees C. Additionally, serum-dependent binding at 37 degrees C was weak when compared to the serum-dependent attachment at 0 degrees C. Pre-incubation at 37 degrees C of cells together with serum did not abolish binding of freshly added rHBsAg at 0 degrees C. However, pre-incubation of rHBsAg with serum at 37 degrees C reduced attachment to cells following incubation at 0 degrees C. Soluble CD14 and LBP, two serum proteins which can act as phospholipid transfer molecules, were shown not to be responsible for the inhibitory effect. Pre-incubation at 37 degrees C of rHBsAg in serum-free hepatoma cell line-conditioned media resulted in a pronounced reduction in subsequent binding to cells at 0 degrees C. These observations suggest that the temperature-dependent inhibitory effect is caused by serum factors that are probably secreted by hepatocytes.


Subject(s)
Hepatitis B Surface Antigens/immunology , Monocytes/immunology , Serum/immunology , Temperature , Acute-Phase Proteins , Animals , CHO Cells , Carrier Proteins , Cell Line, Tumor , Cricetinae , Culture Media, Conditioned , Hepatitis B Surface Antigens/biosynthesis , Hepatitis B Surface Antigens/genetics , Humans , Lipopolysaccharide Receptors , Membrane Glycoproteins , Mice , Protein Binding , Recombinant Proteins/biosynthesis , Saccharomyces cerevisiae/genetics , Saccharomyces cerevisiae/metabolism , Time Factors
2.
Drug Dev Ind Pharm ; 26(4): 391-401, 2000 Apr.
Article in English | MEDLINE | ID: mdl-10769780

ABSTRACT

The results of the stability study of ticlopidine formulations (250 mg and 100 mg) show that products available in many countries worldwide exhibit different stability characteristics. Stability testing under the International Conference on Harmonization (ICH) accelerated test conditions (40 degrees C/75% relative humidity [RH], 3 and 6 months) was performed on a total of 43 products obtained from 18 countries. The samples were visually examined for physical change and analyzed for their content of degradation products, remaining ticlopidine, and in vitro dissolution characteristics (in the case of tablets). Only 6 (16%) of all the samples submitted to this study had a good stability profile. Their appearance remained unchanged during the study; assay results were between 95% and 100%; their impurity content did not exceed 0.25%; and in the dissolution test, at least 75% of ticlopidine was dissolved after 30 min. Three samples had excellent dissolution properties and showed a very high purity level (viz. 21, 40, and 43) over the course of the study.


Subject(s)
Platelet Aggregation Inhibitors/chemistry , Ticlopidine/chemistry , Chromatography, Liquid , Drug Stability , International Cooperation
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