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hepatitis b/albumine
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Serum albumin level as an indicator of response to Hepatitis B vaccination in dialysis patients: A systematic review and meta-analysis.
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UNASSIGNED
Hepatitis B (HB) vaccination is a recommended procedure in all dialysis patients, but its efficacy has not been perfect. In the current study, we aimed to conduct a comprehensive review of the literature to find and pool data of the randomized trials evaluating the impact of serum albumin
[The role of oligomeric structure of human serum albumin during its interaction with polyalbumin receptors in blood serum of patients with viral hepatitis B].
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Several oligomers of human blood serum albumin modified by glutaraldehyde differ in their binding ability to polyalbumin receptors in blood serum of patients with viral hepatitis B. Erythrocytes containing the albumin tetramer are able to agglutinate, while the red blood cells coated with dimer or
Covalent albumin microparticles as an adjuvant for production of mucosal vaccines against hepatitis B.
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Covalently modified albumin (BSA) microparticles were developed for potential use as an adjuvant in mucosal vaccines against hepatitis B. To synthesize consistent protein particles, a covalent approach was proposed to modify BSA. Our strategy was to bond maleic anhydride (MA) molecules to BSA
Interactions between hepatitis B virus and polymeric human albumin. I. Production of monoclonal anti-idiotypes (anti-anti-polymeric human albumin) which recognize hepatitis B virus surface antigen.
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In an attempt to characterize the polymeric human albumin (polyHSA) receptor expressed on hepatitis B virus and hepatocytes, we have used a human anti-polyHSA IgG to generate monoclonal anti-idiotypes (anti-Id) which bear the internal image of polyHSA and mimic its binding activity. Two monoclonal
Removal and inactivation of hepatitis B virus from contaminated pooled plasma in a large-scale manufacturing process for factor VIII and human serum albumin.
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OBJECTIVE
The Japanese Red Cross Society recalled one lot of monoclonal-antibody-purified factor VIII (F VIII) and two lots of human serum albumin (HSA) 5 months after preparation of the final products, because of a procedural error that led to contamination by a unit of plasma positive for
[Binding activity of circulating HBsAg particles for polymerized human albumin in acute hepatitis B].
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The binding activity of circulating HBsAg particles to polymerized human serum albumin (pHSA) was determined by radioimmunoassay in 18 patients with acute hepatitis B at follow-up and compared with other hepatitis B virus (HBV) markers. All patients had serum HBsAg particles with binding sites for
Relationship of large hepatitis B surface antigen polypeptide to human serum albumin.
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A significant proportion (20 to 40%) of highly purified 22-nm hepatitis B surface antigen (HBsAg) particles contain human serum albumin (HSA) as demonstrated by specific precipitation of radioiodinated particles by anti-HSA. Preparations of the isolated major HBsAg polypeptides (P-1, P-2, and P-6)
Regulation of the immune response to hepatitis B virus and human serum albumin. III. Induction of anti-albumin antibody secretion in vitro by C-gene-derived proteins in peripheral B cells from chronic carriers of HBsAg.
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The circulatory pool of B cells from the majority (11/13) of chronic hepatitis B surface antigen (HBsAg) carriers contained sensitized B cells with the capacity to secrete IgG antibodies with specificity for human serum albumin (HSA), when stimulated with E. coli-derived core protein at low
An antibody which precipitates Dane particles in acute hepatitis type B: relation to receptor sites which bind polymerized human serum albumin on virus particles.
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An antibody, which is distinct from the HBsAg- reacts with antigenic sites on Dane particles- HBcAg and HBeAg, was studied by radioimmunoprecipitation of radioactive intact hepatitis B virions in sera obtained early in the course of acute hepatitis type B. The antibody, previously termed anti-Dane
Human liver plasma membranes contain receptors for the hepatitis B virus pre-S1 region and, via polymerized human serum albumin, for the pre-S2 region.
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Hepatitis B virus particles contain three related viral envelope proteins, the small, middle, and large S (surface) proteins. All three proteins contain the small S amino acid sequence at their carboxyl terminus. It is not clear which of these S proteins functions as the viral attachment protein,
An Increased Ratio of Glycated Albumin to HbA1c Is Associated with the Degree of Liver Fibrosis in Hepatitis B Virus-Positive Patients.
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Background. In hepatitis B virus- (HBV-) positive patients, the relationship between the metabolic variables and histological degree of liver fibrosis has been poorly investigated. Methods. A total of 176 HBV-positive patients were assessed in whom the ratios of glycated albumin-to-glycated
A frameshift mutation in the pre-S region of the human hepatitis B virus genome allows production of surface antigen particles but eliminates binding to polymerized albumin.
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The coding region for the major polypeptide (p24S) of hepatitis B surface antigen (HBsAg) is preceded by an in-phase open reading frame termed pre-S. The coding potential of the pre-S region was examined in mouse L cells transformed with cloned hepatitis B virus DNA. Such cells produce three
Hemagglutination assay of polypeptide coded by the pre-S region of hepatitis B virus DNA with monoclonal antibody: correlation of pre-S polypeptide with the receptor for polymerized human serum albumin in serums containing hepatitis B antigens.
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The receptor for polymerized human as well as chimpanzee serum albumins has been identified on the 55-amino acid polypeptide coded by the pre-S region of hepatitis B virus DNA. Monoclonal antibodies were raised against a synthetic polypeptide of 19 amino acid residues representing a hydrophilic
Inhibition of hepatitis B virus replication by vidarabine monophosphate conjugated with lactosaminated serum albumin.
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Vidarabine (ara A) produces severe dose-dependent side-effects. To examine whether its monophosphate ester (ara-AMP) can be effective in the treatment of chronic hepatitis B when given in reduced dosage as a conjugate with lactosaminated human serum albumin (L-HSA), which selectively enters
Mapping of immunodominant B-cell epitopes and the human serum albumin-binding site in natural hepatitis B virus surface antigen of defined genosubtype.
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Twelve MAbs were generated by immunization of BALB/c mice with plasma-derived hepatitis B virus surface spherical antigen particles subtype ayw2 (HBsAg/ayw2 genotype D). Their epitopes were mapped by analysis of reactivity with plasma-derived HBsAg/ayw2 and HBsAg/adw2 (genotype A) in enzyme
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