Results 211 to 220 of about 5,594 (243)

Inherited Sialoglycoprotein Deficiencies in Human Erythrocytes of Type En(a ‐)

British Journal of Haematology, 1977
We have investigated the membranes of erythrocytes from a family in which there is a genetic defect (previously described as the En(a ‐) condition) resulting in the loss of the major erythrocyte sialoglycoprotein (PAS‐1). The results show that two different types of sialoglycoprotein deficiency can be distinguished within this family.
David J. Anstee, Michael J. A. Tanner, Diana M. Barker, P A Judson   +3 more
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THE REGIONAL DISTRIBUTION OF SIALOGLYCOPROTEINS, GANGLIOSIDES AND SIALIDASE IN BOVINE BRAIN

Journal of Neurochemistry, 1970
Abstract— Sialoglycoproteins and gangliosides were characterized in various bovine brain regions by determining the amount of sialic acid. Expressed per g dry weight, the gangliosidic sialic acid ranged from 11·20 to 1·93 μmol and the glycoprotein sialic acid from 8·93 to 1·84 μmol in grey and white matter respectively (values not corrected for ...
J. Heijlman, P. A. Roukema
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Hybrid sialoglycoprotein content of St(a+) red cells

Transfusion, 1988
St(a+) red cells contain a ficin‐resistant hybrid sialoglycoprotein (SGP) consisting of the amino terminus of Ss sialoglycoprotein (Ss SGP) and the carboxyl terminus of MN sialoglycoprotein (MN SGP). Ficin‐ modified St(a+) but not St(a−) red cells were agglutinated by monoclonal antibodies NN5 (anti‐N) and 31 (detecting a sialic acid‐ dependent ...
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Fractionation of sialoglycoproteins on an immobilized sialic acid-binding lectin

Analytical Biochemistry, 1981
Abstract Carcinoscorpin, the sialic acid-binding lectin from the horseshoe crab Carcinoscorpius rotunda cauda , has been immobilized using Sepharose. The immobilized lectin is shown to resolve the isoenzymes of alkaline phosphatase from sheep brain based on the difference in their sialic acid contents.
B.K. Bachhawat, Subal Bishayee, D.Thambi Dorai   +2 more
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Nucleotide pyrophosphatase, a sialoglycoprotein located on the hepatocyte surface

Nature, 1974
A sialoglycoprotein enzyme hydrolysing nucleotide pyrophosphate bonds is a major externally located component on the hepatocyte surface membrane.
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Hageman factor, a novel sialoglycoprotein with esterase activity

Biochimica et Biophysica Acta (BBA) - Mucoproteins and Mucopolysaccharides, 1965
A novel esterase has been isolated from bovine plasma in a highly purified form. According to electrophoresis and ultracentrifugal sedimentation patterns it represents a homogeneous 7.1 S sialoglycoprotein being composed of 5.9% neutral carbohydrates, 4.8% aminosugars and 4.4% sialic acid.
John G.G. Schoenmakers, R. Matze, Clemens Haanen, F. Zilliken   +3 more
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Human erythrocyte membrane sialoglycoproteins: A study of interconversion

Biochemical and Biophysical Research Communications, 1974
Summary The sialoglycoproteins of human erythrocyte membranes can be separated into four molecular weight classes by gel electrophoresis in the presence of sodium dodecyl sulfate. Two of these components participate in an aggregation/disaggregation equilibrium favoring the lower molecular weight form at higher temperature.
Martin Morrison, Jean K. Tuech
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SIALOGLYCOPROTEINS AND SEVERAL GLYCOSIDASES IN DEVELOPING RAT BRAIN

Journal of Neurochemistry, 1970
Abstract— The amount of sialoglycoproteins expressed as μmol of sialic acid per g of lipid‐free residue remained fairly constant in developing rat brain. However, the activity of various enzymes which may be involved in glycoprotein metabolism varied in an inconstant fashion during the period of development.
Richard H. Quarles, Roscoe O. Brady
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Interactions between a membrane sialoglycoprotein and planar lipid bilayers [PDF]

The Journal of Membrane Biology, 1978
Bilayer membranes formed from lipids dissolved in decane were exposed to glycophorin, a sialoglycoprotein which had been extracted from human red cell membranes. The interaction with the bilayer produced an increase in the steady state electrical conductance of the membrane proportional to the amount added.
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Characterization of the Ss sialoglycoprotein and its antigens in Rhnull erythrocytes

Blut, 1987
The Ss sialoglycoprotein (glycophorin B) and its antigens in Rhnull erythrocytes, which lack the Rhesus blood group antigens, due to apparently silent (amorphic type) or independent suppressor (regulator type) genes, were investigated. The quantity of the molecule in amorphic and in regulator type red cell membranes was found to be decreased by about ...
W. Dahr, J. Moulds, W. Gielen, L. Lebeck, J. Krüger, M. Kordowicz   +5 more
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