Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.1.53 (sialidase)
 2,694 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Immunoblotting with two examples of anti-Dha to the electrophoretically separated components of antigen-positive membranes gave a positive reaction with a component of the same apparent Mr (40,000) as sialoglycoprotein beta (SGP beta, syn: glycoconnectin, glycophorin C). The Dha antigenic determinant was sensitive to trypsin, but resistant to chymotrypsin and Endo F. By immunoblotting, one anti-Dha failed to react with sialidase-treated Dh(a+) cells, whilst the other gave a positive result. In contrast, neither antibody agglutinated sialidase-treated red cells. SGP beta was precipitated from Dh(a+) and Dh(a-) phenotype red cells by monoclonal anti-beta (NBTS/BRIC 10). SGP beta from Dh(a+) but not from Dh(a-) red cells was stained by immunoblotting with anti-Dha. These results assign the Dha antigenic epitope to SGP beta.
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PMID:Immunochemical characterisation of the low-incidence antigen, Dha. 171 1

The Ina and Inb blood group antigens were found to be located on an erythrocyte membrane glycoprotein of 80,000 MW by immunoblotting with human anti-Ina and anti-Inb antibodies under non-reducing conditions. This glycoprotein is shown here to be identical to that defined by monoclonal antibodies to CDw44, and a new murine monoclonal antibody (BRIC 35) is added to this cluster. Experiments with endo-beta-galactosidase and Endo F preparations suggest that the glycoprotein contains one or more N-glycans but that these oligosaccharides do not contain extensive poly-N-acetyllactosaminyl sequences. Experiments using membranes prepared from sialidase-treated normal erythrocytes, from Tn erythrocytes and from Cad erythrocytes suggest that the glycoprotein does not contain a substantial content of O-glycans. The Inb antigen and the epitope defined by a murine monoclonal antibody (BRIC 35) show reduced expression on Lu(a-b-) erythrocytes which result from the effect of the dominant inhibitor gene In(Lu). Evidence is presented here that the Inb antigen is expressed on normal granulocytes and lymphocytes and on the haemopoietic cell lines HEL, K562 and HL-60, a lymphoblastoid cell line and lymphocytes from two patients with B-CLL.
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PMID:The Ina and Inb blood group antigens are located on a glycoprotein of 80,000 MW (the CDw44 glycoprotein) whose expression is influenced by the In(Lu) gene. 245 87

Aluminium (Al) in the blood is bound to transferrin (Tf), a glycoprotein of about 80kDa that is characterized by its need for a synergistic anion. In this focused review, the binding affinity of Al to Tf is surveyed in the context of our recent studies using on-line high-performance liquid chromatography/high-resolution inductively coupled plasma mass spectrometry (HPLC/HR-ICP-MS). Al in human serum without any in vitro Al-spikes was present in a form bound to the N-lobe site of Tf. The influences of sialic acid in the carbohydrate chain of human serum Tf (hTf) were studied using asialo-hTf, obtained by treatment with sialidase. The binding affinity of Fe was similar between asialo-hTf and native-hTf, while that of Al for asialo-hTf was larger than that for native-hTf, especially in the presence of oxalate, a synergistic anion. The above findings are discussed in relation to diseases in which the serum concentrations of carbohydrate-deficient Tf and oxalate are augmented.
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PMID:Binding affinity of aluminium to human serum transferrin and effects of carbohydrate chain modification as studied by HPLC/high-resolution ICP-MS--speciation of aluminium in human serum. 1613 93