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beta d galactose/hepatitis
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[Alteration of the glycan profile of serum glycoproteins during the seroconversion process in hepatitis B virus-infected patients treated with antiviral therapy and its clinical significance].
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OBJECTIVE
To use a lectin microarray to study the alteration of glycan affinity profiles of serum glycoproteins during the hepatitis B e antigen (HBeAg) and hepatitis B surface antigen (HBsAg) seroconversion in patients with chronic hepatitis B (CHB) following treatment with antiviral therapy,and to
Antibody to epiglycanin and radioimmunoassay to detect epiglycanin-related glycoproteins in body fluids of cancer patients.
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By means of a radioimmunoassay, which utilized [125I]-epiglycanin and anti-epiglycanin antiserum induced in rabbits by injections of viable TA3-Ha ascites cells with Freund's complete adjuvant, picogram quantities of epiglycanin could be detected. Anti-epiglycanin antiserum was similarly produced in
Allomyrina dichotoma lectin-nonreactive alpha-fetoprotein in hepatocellular carcinoma and other tumors: comparison with Ricinus communis agglutinin-I.
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Allomyrina dichotoma lectin (allo A) with a specificity to beta-D-galactose was used to fractionate human alpha-fetoprotein (AFP) by affinity electrophoresis. AFP from cord sera and serum of a patient with fulminant hepatitis showed single bands with a high affinity for allo A. Some patients with
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