A Single Point Mutation Reverses the Donor Specificity of Human Blood Group B-synthesizing Galactosyltransferase
نویسندگان
چکیده
منابع مشابه
A case of weak blood group B expression (Bm) associated with abnormal blood group galactosyltransferase.
The mechanisms of unusually weak A and B blood group expressions have not been well understood. Since the human blood group A and B substances are produced by the action of blood group GalNAc transferase and Gal transferase, respectively, the mechanism may be elucidated by examining the properties of the blood group transferases and membranes of the subjects with the abnormality. We examined a ...
متن کاملSuppressed expression of blood group B antigen and blood group galactosyltransferase in a preleukemic subject.
The B antigen activity was severely diminished in a patient's RBCs at the preleukemic stage prior to chemo- or radiotherapy. The amount of H sites of the patient's RBC membranes was found to be comparable to that of O RBC membranes. The activity of alpha (1----2) fucosyltransferase (H enzyme) was not severely decreased in the patient's plasma and bone marrow. However, the activity of alpha (1--...
متن کاملBinding of an acceptor substrate analog enhances the enzymatic activity of human blood group B galactosyltransferase.
The hydrolysis of the donor substrate uridine diphosphate galactose (UDP-Gal) by human blood group B galactosyltransferase (GTB) has been followed by nuclear magnetic resonance in the presence and in the absence of an acceptor substrate analog. It is observed that the presence of the acceptor substrate analog promotes hydrolysis of UDP-Gal. Subsequent analysis of the kinetics of the enzymatic h...
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Background: Cholera toxin B subunit (CTB) has been extensively considered as an immunogenic and adjuvant protein, but its yield of expression is not satisfactory in many studies. The aim of this study was to compare the expression of native and mutant recombinant CTB (rCTB) in pQE vector. Methods: ctxB fragment from Vibrio cholerae O1 ATCC14035 containing the substitution of mutant ctxB for ami...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2003
ISSN: 0021-9258
DOI: 10.1074/jbc.m212002200