Alkali-labile oligosaccharides from glycoproteins of different erythrocyte and milk fat globule membranes.
Abstract: 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 disaccharide plus two molecules of sialic acid. Periodate oxidation together with paper chromatography of alkaline degraded fragments showed these two molecules of sialic acid to be linked to positions C3 and C6 of the galactosyl and N-acetylgalactosamine residues respectively. Evidence was obtained for a similar structure from pig and cow erythrocyte glycoproteins and human milk fat globule membrane glycoproteins although the complete structure was not elucidated. In all native glycoprotein fractions, the unsubstituted disaccharide beta-D-galactosyl (1-3)-N-acetyl-D-galactosamine was found to be present to different extents. Haemagglutination inhibition tests against human anti-T serum, Arachis hypogoea and Vicia graminea by desialylated glycoproteins showed the presence of the T-antigen, confirming the chemical findings. Inhibition was found to be proportional to the chemically detected amounts of disaccharide in each fraction. Evidence for a second carbohydrate chain in horse, sheep and human erythrocyte glycoproteins with a sialic acid substituted N-acetylgalactosamine residue as the terminal sequence was obtained using the agglutinin from Helix pomatia.
Publication Date: 1976-09-07 PubMed ID: 963062DOI: 10.1016/0005-2736(76)90460-0Google Scholar: Lookup
The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
- Comparative Study
- Journal Article
Summary
This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.
This research article examines the chemical composition of glycoproteins found in different animal erythrocyte and human milk fat globule membranes. The study found a significant amount of a specific disaccharide in most samples, with the presence of the T-antigen confirmed through haemagglutination inhibition tests.
Objective and Method of the Research
- The main goal of this research was to investigate the presence of a certain disaccharide (beta-D-galactosyl (1-3)-N-acetyl-D-galactosaminital) in glycoproteins from different animal erythrocyte (red blood cell) membranes and human milk fat globule membranes.
- To do this, the researchers extracted glycoproteins from horse, sheep, cow, pig and human erythrocyte membranes and human milk fat globule membranes using a phenol extraction technique.
- These extracted glycoproteins were then examined by gas chromatography to detect the presence of the said disaccharide after throwing them under alkaline borohydride treatment.
Findings of the Research
- The study found that all glycoprotein fractions revealed the presence of the disaccharide in question. Nonetheless, cow and pig erythrocyte membrane glycoproteins were found to contain much lesser amounts compared to other species.
- A tetrasaccharide was isolated from horse and sheep glycoproteins which included the disaccharide along with two molecules of sialic acid.
- Further periodate oxidation and paper chromatography investigations elucidated that these two molecules of sialic acid were linked to positions C3 and C6 of the galactosyl and N-acetylgalactosamine residues respectively.
- Pig and cow erythrocyte glycoproteins and human milk fat globule membrane glycoproteins also showed evidence of similar linkage structures, although the complete structure was not conclusively determined.
- Haemagglutination inhibition tests confirmed the presence of the T-antigen in the desialylated glycoproteins, with inhibition found proportional to the chemically detected amounts of the disaccharide in each fraction.
- Some evidence pointed to the existence of a second carbohydrate chain in horse, sheep, and human erythrocyte glycoproteins. This additional chain was found to carry a sialic acid substituted N-acetylgalactosamine residue as the terminal sequence. This finding was obtained using the agglutinin from Helix pomatia.
Cite This Article
APA
Glöckner WM, Newman RA, Dahr W, Uhlenbruck G.
(1976).
Alkali-labile oligosaccharides from glycoproteins of different erythrocyte and milk fat globule membranes.
Biochim Biophys Acta, 443(3), 402-413.
https://doi.org/10.1016/0005-2736(76)90460-0 Publication
Researcher Affiliations
MeSH Terms
- Animals
- Cattle
- Female
- Glycoproteins / analysis
- Hemagglutination Inhibition Tests
- Hexosamines / analysis
- Hexoses / analysis
- Horses
- Humans
- Milk Proteins
- Milk, Human / analysis
- Oligosaccharides / analysis
- Pregnancy
- Sheep
- Sialic Acids / analysis
- Species Specificity
- Swine
Citations
This article has been cited 8 times.- Kusui K, Takasaki S. Structural study of N-linked sugar chains of sheep erythrocyte membrane glycoproteins.. Glycoconj J 1998 Jan;15(1):3-10.
- Fischer J, Klein PJ, Farrar GH, Hanisch FG, Uhlenbruck G. Isolation and chemical and immunochemical characterization of the peanut-lectin-binding glycoprotein from human milk-fat-globule membranes.. Biochem J 1984 Dec 1;224(2):581-9.
- Unger P, Procter JL, Moulds JJ, Moulds M, Blanchard D, Guizzo ML, McCall LA, Cartron JP, Dahr W. The Dantu erythrocyte phenotype of the NE variety. II. Serology, immunochemistry, genetics, and frequency.. Blut 1987 Jul;55(1):33-43.
- Dahr W, Kordowicz M, Moulds J, Gielen W, Lebeck L, Krüger J. Characterization of the Ss sialoglycoprotein and its antigens in Rhnull erythrocytes.. Blut 1987 Jan;54(1):13-24.
- Heeb MJ, Marini AM, Gabriel O. Factors affecting binding of galacto ligands to Actinomyces viscosus lectin.. Infect Immun 1985 Jan;47(1):61-7.
- Latron F, Blanchard D, Cartron JP. Immunochemical characterization of the human blood cell membrane glycoprotein recognized by the monoclonal antibody 12E7.. Biochem J 1987 Nov 1;247(3):757-64.
- Klein PJ, Newman RA, Müller P, Uhlenbruck G, Schaefer HE, Lennartz KJ, Fischer R. Histochemical methods for the demonstration of Thomsen-Friedenreich antigen in cell suspensions and tissue sections.. Klin Wochenschr 1978 Aug 1;56(15):761-5.
- Farrar GH, Harrison R. Isolation and structural characterization of alkali-labile oligosaccharides from bovine milk-fat-globule membrane.. Biochem J 1978 Jun 1;171(3):549-57.
Use Nutrition Calculator
Check if your horse's diet meets their nutrition requirements with our easy-to-use tool Check your horse's diet with our easy-to-use tool
Talk to a Nutritionist
Discuss your horse's feeding plan with our experts over a free phone consultation Discuss your horse's diet over a phone consultation
Submit Diet Evaluation
Get a customized feeding plan for your horse formulated by our equine nutritionists Get a custom feeding plan formulated by our nutritionists
