Results 211 to 220 of about 4,387 (243)
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Erythrocyte sialoglycoproteins and Plasmodium falciparum invasion

Transactions of the Royal Society of Tropical Medicine and Hygiene, 1983
Human erythrocytes with a deficiency in glycophorin A (En(a-) cells) and glycophorin B (S-s-U- and S-s-U+ cells) show significant resistance in vitro to invasion by Plasmodium falciparum merozoites. Treatment of normal erythrocytes with trypsin and chymotrypsin also reduced invasion.
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Isolation of murine sialoglycoprotein using consecutive chromatography

Life Sciences, 1991
Affinity columns and high performance liquid chromatography were employed consecutively to obtain 89, 65, 46 and 29 kilodalton sialoglycoproteins from mouse erythrocyte ghosts free of the Band 3 protein which traditionally co-purifies with these proteins.
Donella J. Wilson, JoséM. Planas
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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   +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   +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   +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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