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Topic:Glycoproteins

Glycoproteins are molecules composed of carbohydrates covalently bonded to proteins, found throughout various tissues and fluids in horses. These molecules are involved in numerous biological processes, including cell-cell interactions, immune function, and structural integrity of tissues. Glycoproteins in horses can be studied to understand their roles in health and disease, as well as their potential as biomarkers for various conditions. Research in this area explores the structure, function, and regulatory mechanisms of glycoproteins, as well as their implications in equine medicine. This page compiles peer-reviewed research studies and scholarly articles that investigate the significance and applications of glycoproteins in equine biology and veterinary science.
Structural proteins of equine infectious anemia virus and their antigenic activity.
American journal of veterinary research    January 1, 1984   Volume 45, Issue 1 5-10 
Nishimura M, Nakajima H.Using purified equine infectious anemia (EIA) virus labeled with 3H-glucosamine or 14C-protein hydrolysate, structural proteins were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. As a result, 2 glycoproteins and 10 proteins with molecular weights (mol wt) ranging from 12,000 to 115,000 daltons were demonstrated. Of 12 structural proteins, 3 proteins, namely a glycoprotein with mol wt of 76,000 (gp76) and 2 proteins with mol wt of 25,000 (p25) and 12,000 (p12), respectively, had distinct antigenic activity from one another in immunodiffusion. Development of antibodies a...
Effects of common radioiodination procedures on the binding of glycoproteins to immobilized lectins.
Biochemical and biophysical research communications    January 14, 1983   Volume 110, Issue 1 103-107 doi: 10.1016/0006-291x(83)91266-4
Montelaro RC, West M, Ivey M.Representative glycoproteins including fetuin, protein A, ovalbumin, alpha 1 acid glycoprotein, and the major glycoprotein of equine infectious anemia virus were labelled with 125I by the chloramine-T or Bolton-Hunter procedure and their binding to immobilized Con A or lentil lectin compared to untreated samples of each glycoprotein. Glycoprotein modification was no greater than one substituted residue per protein molecule. Yet the radioiodinated glycoproteins typically displayed only 0-50% of the lectin binding observed with untreated samples. These results indicate that lectin glycoprotein b...
Immunochemical studies of infectious mononucleosis–XI. comparison of heterophile antibody inhibitors from the erythrocyte membranes of four mammalian species.
Molecular immunology    January 1, 1983   Volume 20, Issue 1 1-10 doi: 10.1016/0161-5890(83)90099-8
Latif ZA, Fletcher MA.Immunochemical comparisons were made of the reactivity of membrane glycoproteins from horse, bovine, sheep and goat erythrocytes with heterophile antibodies of infectious mononucleosis. The four receptors were tested as competitive inhibitors of a sandwich-type solid-phase radioimmunoassay and of agglutination of glycoprotein-latex reagents by infectious mononucleosis serum. The results of this study showed that the bovine glycoprotein had a superior reactivity with this heterophile antibody system and sheep erythrocyte glycoprotein was the least reactive. The latter had negligible ability to ...
Comparison of receptor properties of erythrocyte membrane glycoproteins.
Developmental and comparative immunology    January 1, 1982   Volume 6, Issue 4 765-774 
Klimas NG, Caldwell KE, Whitney PL, Fletcher MA.Membrane glycoproteins from horse, sheep, goat and bovine erythrocytes were solubilized and purified. These glycoproteins could be placed in three groups based on their degrees of glycosylation: The major bovine erythrocyte glycoprotein (BGII) had 77% sugar, the minor bovine glycoprotein (BGI) had 27% sugar and the others had approximately 50% sugar. Four of the glycoproteins aggregated in a uniform way in aqueous solution--one, BGII, did not. Four had similar subunit sizes of 25-34,000 daltons, but BGII was larger--55,000 daltons. Receptor functions (for plant and invertebrate lectins, antibo...
Some aspects of tissue maturation in fetal and perinatal foals.
Journal of reproduction and fertility. Supplement    January 1, 1982   Volume 32 589-595 
Barnard K, Leadon DP, Silver IA.Collagen, elastin and structural glycoprotein content of the lungs of 38 fetal and neonatal foals, 8 of which were showing dysmaturity or convulsive syndrome, were measured by standard biochemical means. Glycoprotein content showed little or no change between 100 and 340 days of gestation; elastin remained constant from 100 to about 260 days when there was an exponential increase up to the time of birth, while collagen content rose linearly from 100 days to birth. In dysmature animals there was significantly less collagen in the lungs at birth but the difference in elastin content between the ...
Equine follicle-stimulating hormone. Purification, acid dissociation, and binding to equine testicular tissue.
The Journal of biological chemistry    September 25, 1981   Volume 256, Issue 18 9567-9572 
Combarnous Y, Hengé MH.A simple method of purification of equine follicle-stimulating hormone is described by which two forms of the hormone are obtained. The acid dissociation of the most active preparation was studied and a pKa of 5.8 was determined at 37 degrees C. This value is 2 pH units higher than that observed for pregnant mare serum gonadotropin suggesting that the binding areas between subunits are not identical in the two hormones. We also describe an homologous radioreceptor assay of equine follicle-stimulating hormone which is highly specific for this hormone in contrast to the heterologous systems desc...
[Effect of 2 methods of demineralization on the on the preservation of glycoproteins and proteoglycans in the intertubular and peritubular dentin in the horse].
Journal de biologie buccale    December 1, 1980   Volume 8, Issue 4 315-330 
Goldberg M, Molon Noblot M, Septier D.The effect of 2 methods of demineralization on the preservation of proteoglycans and glycoproteins was studied in the intertubular and peritubular dentine of the horse. The specimens embedded in Epon were demineralized with a 2% acid formic solution (Bonucci and Gheradi, 1975). Other fragments were treated with an organic solution of EDTA alkylammonium salt (Scott and Kyffin, 1979). These methods preserved in a satisfactory way these labile organic components. In the intertubular dentine, glycoproteins and proteoglycans were also identified, either associated with collagen fibres as a glue and...
Identification by gas-liquid chromatography-mass spectrometry of 4-O-acetyl-9-O-lactyl-N-acetyl-neuraminic acid, a new sialic acid from horse submandibular gland.
Biochimica et biophysica acta    June 19, 1980   Volume 630, Issue 2 306-310 doi: 10.1016/0304-4165(80)90435-3
Reuter G, Pfeil R, Kamerling JP, Vliegenthart JF, Schauer R.The novel sialic acid 4-O-acetyl-9-O-lactyl-N-acetylneuraminic acid has been identified as a constituent of horse submandibular gland glycoproteins in addition to the already known equine sialic acids, N-acetylneuraminic acid, 4-O-acetyl-N-acetylneuraminic acid, 9-O-acetyl-N-acetylneuraminic acid, 4,9-di-O-acetyl-N-acetylneuraminic acid, N-glycolylneuraminic acid, 4-O-acetyl-N-glycolylneuraminic acid and 9-O-acetyl-N-glycolylneuraminic acid. The structure has been established by combined gas-liquid chromatography-mass spectrometry.
Purification by affinity chromatography and characterization of a neutral alpha-glucosidase from horse kidney.
Biochimica et biophysica acta    March 14, 1980   Volume 612, Issue 1 85-96 doi: 10.1016/0005-2744(80)90281-8
Giudicelli J, Emiliozzi R, Vannier C, de Burlet G, Sudaka P.A horse kidney neutral alpha-D-glucosidase (alpha-D-glucoside glucohydrolase, EC 3.2.1.20) was purified about 580-fold with a yield of 33% by an affinity chromatography technique using the p-aminophenyl-beta-D-maltoside, a substrate derivative, as ligand. The purified enzyme, homogeneous in polyacrylamide gel electrophoresis, was a glycoprotein with a molecular weight of 280 000 as calculated by gel filtration and its isoelectric focusing points was found to be pH 4.1. The purified enzyme was able to hydrolyze various substrates having (alpha-1,2), (alpha-1,3), (alpha-1,4), and (alpha-1,6) glu...
The lectin-binding sites of the erythrocyte membrane components of horse, swine and sheep. Characterization by their molecular weights.
Hoppe-Seyler's Zeitschrift fur physiologische Chemie    March 1, 1979   Volume 360, Issue 3 421-428 doi: 10.1515/bchm2.1979.360.1.421
Gürtler LG, Yeboa DA, Cleve H.The membrane components of equine, porcine and ovine erythrocytes were separated by sodium dodecylsulfate polyacrylamide gel electrophoresis and subsequently incubated with the radioiodinated lectins from lentils (LCH), castorbeans (RCA), Phaseolus beans (L-PHA), gorse seeds (UEH-F) and from vineyard snails (HPA). The following individual glycoproteins could be labeled: gp 26, 33, 100 and 320 in horse erythrocytes, gp 24, 46, 75, 130 and 210 in swine and gp 24, 57, 100 and 210 in sheep erythrocytes.
Seasonal changes in hematological indices, protein and glycoprotein levels and in activity of some enzymes in Arabian horses.
Bulletin de l'Academie polonaise des sciences. Serie des sciences biologiques    February 1, 1979   Volume 26, Issue 10 719-723 
Gill J, Szwarocka-Priebe T, Krupska U, Pepłowska Z.No abstract available
Alkali-labile oligosaccharides from glycoproteins of different erythrocyte and milk fat globule membranes.
Biochimica et biophysica acta    September 7, 1976   Volume 443, Issue 3 402-413 doi: 10.1016/0005-2736(76)90460-0
Glöckner WM, Newman RA, Dahr W, Uhlenbruck G.Phenol extraction of horse, sheep, cow, pig and human erythrocyte membranes and human milk fat globule membranes gave glycoprotein fractions, all of which were shown by gas chromatography to contain the reduced disaccharide beta-D-galactosyl (1-3)-N-acetyl-D-galactosaminital after treatment with alkaline borohydride. Cow and pig erythrocyte membrane glycoproteins were found however to contain much lower amounts than the erythrocyte membrane glycoproteins of the other species tested. After gel filtration, a tetrasaccharide was isolated from horse and sheep glycoproteins containing the disacchar...
Immunochemical studies on blood groups. Purification, chemical and immunochemical properties of blood group-active glycoproteins from horse gastric mucosae.
Archives of biochemistry and biophysics    February 1, 1976   Volume 172, Issue 2 510-523 doi: 10.1016/0003-9861(76)90104-1
Newman W, Kabat EA.No abstract available
Characterization of human, bovine, and horse antithrombin III.
Biochemistry    January 27, 1976   Volume 15, Issue 2 368-373 doi: 10.1021/bi00647a020
Kurachi K, Schmer G, Hermodson MA, Teller DC, Davie EW.A comparison of the physical-chemical properties of human, bovine, and horse antithrombin III has been made. These three plasma proteins are strong inhibitors of bovine factor Xa and form a 1:1 molar complex with this coagulation enzyme. Human, bovine, and horse antithrombin III are glycoproteins containing hexose, hexosamine, and neuraminic acid. The total carbohydrate was 9, 12, and 16% for human, bovine, and horse antithrombin III, respectively. These proteins have a similar amino acid composition, although some monor variations were noted. Each antithrombin III is composed of a single poly...
Isolation and partial characterization of the major glycoproteins of horse and swine erythrocyte membranes.
Biochimica et biophysica acta    October 6, 1975   Volume 406, Issue 2 206-213 doi: 10.1016/0005-2736(75)90005-x
Fujita S, Cleve H.The major glycoproteins of horse and swine erythrocyte membranes were isolated and examined chemically and immunologically. The major glycoprotein of horse erythrocyte membranes had a molecular weight of 33 000 and consisted of 46.2% protein and 53.8% carbohydrate, of which 9.4% was hexose, 10.1% hexosamine and 33.7% sialic acid. This glycoprotein was associated with activity for the infectious mononucleosis heterophile antigen. There were two different major glycoproteins in swine erythrocyte membranes. One major glycoprotein had a molecular weight of 46 200 and consisted of 34.2% protein and...
Species variability in the modification of erythrocyte surface proteins by enzymatic probes.
Biochimica et biophysica acta    March 13, 1975   Volume 382, Issue 2 181-192 doi: 10.1016/0005-2736(75)90176-5
Carraway KL, Colton DG, Shin BC, Triplett RB.Bovine and equine erythrocytes have been studied by three different surface modification techniques to investigate the accessibility of the surface components to the external medium. Lactoperoxidase labeling of equine erythrocytes results in a significant labeling of only one membrane component, a 100 000-mol.wt polypeptide corresponding to the membrane-spanning Component III of human erythrocytes. The major sialoglycoprotein of the equine erythrocyte is not labeled. This is in contradistinction to the situation for human and bovine cells, where both components are labeled. The equine membrane...
Molecular weight of the major acidic glycoprotein of horse erythrocyte membrane.
Archives of biochemistry and biophysics    August 1, 1974   Volume 163, Issue 2 581-588 doi: 10.1016/0003-9861(74)90517-7
Hunter SJ, Fletcher MA, Bush CA.No abstract available
Immunochemical studies of infectious mononucleosis. IV. Effect of proteases on the glycoprotein of horse erythrocytes.
Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.)    March 1, 1974   Volume 145, Issue 3 1100-1105 doi: 10.3181/00379727-145-37961
Fletcher MA, Lo TM, Levey GS.No abstract available
Serial measurements of serum protein, glycoprotein, and lipoprotein fractions in normal and Venezuelan equine encephalomyelitis-vaccinated ponies and burros.
American journal of veterinary research    February 1, 1972   Volume 33, Issue 2 323-327 
Rollins JB, Shultz TD, Fiser RH.No abstract available
Studies on the serum glycoproteins level in mares in early pregnancy.
Bulletin de l'Academie polonaise des sciences. Serie des sciences biologiques    January 1, 1965   Volume 13, Issue 8 485-487 
Wójcik K, Ewy Z.No abstract available
[Modifications of blood glycoprotein levels during immunization by tetanus anatoxin in horse].
Comptes rendus hebdomadaires des seances de l'Academie des sciences    August 12, 1957   Volume 245, Issue 7 810-812 
DELAUNAY A, HENON M, BRUYET P, MEIGNIEN C, RECULARD P.No abstract available