Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.1 (chymotrypsin)
 10,938 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Human anti-S and anti-s eluates bound to glycophorin B on immunoblots from membranes of S+ and s+ red cells, respectively. Eluates of human anti-S were more efficiently prepared from sensitized trypsin-treated cells than from sensitized untreated cells. The results of immunoblotting membranes from enzyme-treated cells confirmed the serological findings: S and s antigens were not affected by treatment with trypsin or sialidase but were destroyed or much depressed by treatment with papain, pronase or alpha-chymotrypsin. Immunoblotting with anti-S or anti-s of membranes from cells with unusual MNS phenotypes confirms the involvement of glycophorin B in hybrid glycophorins; the existence of such hybrid glycophorins was deduced previously from serological work or immunoblotting with monoclonal antibodies. The presence of s-active glycophorin B in glycophorin (B-A)Dantu, in glycophorin BMiIII and in glycophorin (A-B)MiV was confirmed. The bands observed when Mit+ membranes were immunoblotted with anti-S supports the suggestion from serological work that the Mit antigen is associated with an altered S antigen.
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PMID:Immunoblotting of human red cell membranes: detection of glycophorin B with anti-S and anti-s antibodies. 239 72

MNS antigens are carried on glycophorin A (GPA), glycophorin B (GPB), or their variants. Antigens at the N-terminus of GPA are sensitive to cleavage by ficin, papain, and trypsin but are resistant to alpha-chymotrypsin. Antigens at the N-terminus of GPB are sensitive to cleavage by ficin, papain, and alpha-chymotrypsin but are resistant to trypsin treatment. These characteristics have been used to aid in the identification of blood group alloantibodies. Recent molecular analyses have identified changes in amino acids that are associated with several low-incidence antigens in the MNS blood group system. This review relates the molecular studies with the susceptibility or resistance of these antigens to treatment of intact red blood cells by proteolytic enzymes.
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PMID:Low-incidence MNS antigens associated with single amino acid changes and their susceptibility to enzyme treatment. 1537 83

The low-prevalence MNS blood group antigenTSEN is located at the junction of glycophorin A (GPA) to glycophorin B (GPB) in several hybrid glycophorin molecules. Extremely rare people have RBCs with a double dose of the TSEN antigen and have made an antibody to a high-prevalence MNS antigen. We report the first patient who is heterozygous for GYP.JL and Mk. During prenatal tests,an alloantibody to a high-prevalence antigen was detected in the serum of a 21-year-old Hispanic woman. The antibody detected an antigen resistant to treatment by papain, trypsin, alpha-chymotrypsin, or DTT. The antibody was strongly reactive by the IAT with all RBCs tested except those having the MkMk, GP.Hil/GP.Hil, or GP.JL/GP.JL phenotypes. The patient's RBCs typed M+N-S+/-s-U+, En(a+/-), Hut-, Mi(a-), Mur-, Vw-, Wr(a-b-), and were TSEN+, MINY+. Reactivity with Glycine soja suggested that her RBCs had a decreased level of sialic acid. Immunoblotting showed the presence of monomer and dimer forms of a GP(A-B) hybrid and an absence of GPA and GPB. Sequencing of DNA and PCR-RFLP using the restriction enzyme RsaI confirmed the presence of a hybrid GYP(AB). The patient's antibody was determined to be anti-EnaFR. She is the first person reported with the GP.JL phenotype associated with a deletion of GYPA and GYPB in trans to GYP.JL.
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PMID:An alloantibody to a high-prevalence MNS antigen in a person with a GP.JL/Mk phenotype. 1828 4