Studies on a Glycopeptide From Ovalbumin

Clamp, J. R.; Hough, L.

doi:10.1042/bj0940502

Cited by 30 publications

(12 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…During the oxidation, formic acid was released; rapid formation of this acid corresponded to the oxidation of non-reducing terminal mannosyl groups, and the slower release over a subsequent period of 12 days was probably because of the oxidation of amino acid residues. Similar slow progressive oxidations have been reported for glycopeptides of y-globulin (Rothfus & Smith, 1962;Clamp & Hough, 1965) and for ovalbumin (Fletcher et al 1963).…”

Section: Discussionsupporting

confidence: 75%

The structure of a glycopeptide isolated from the yeast cell wall

Sentandreu

Northcote

1968

Biochemical Journal

177

View full text Add to dashboard Cite

1. Glycopeptides containing mannose were extracted from isolated yeast cell walls by ethylenediamine and purified by treatment with Pronase and fractionation on a Sephadex column. 2. A glycopeptide that appeared homogeneous on electrophoresis and ultracentrifugation had a molecular weight of 76000, and contained a high-molecular-weight mannan and approx. 4% of amino acids. 3. The amino acid composition of the peptide was determined. It was rich in serine and threonine and also contained glucosamine. No cystine and methionine were detected. 4. The glycopeptide underwent a beta-elimination reaction when treated with dilute alkali at low temperatures. The reaction resulted in the release of mannose, mannose disaccharides and possibly other low-molecular-weight mannose oligosaccharides. During the beta-elimination reaction the dehydro derivatives of serine and threonine were formed. One of the linkages between carbohydrate and amino acids in the glycopeptide is an O-mannosyl bond from mannose and mannose oligosaccharides to serine and threonine. 5. After the beta-elimination reaction the bulk of the mannose in the form of the large mannan component was still covalently linked to the peptide. This polysaccharide was therefore attached to the amino acids by a linkage different from the O-mannosyl bonds to serine and threonine that attach the low-molecular-weight sugars. 6. Mannan was prepared from the glycopeptide and from the yeast cell wall by treatment of the fractions with hot solutions of alkali. The mannan contained aspartic acid and glucosamine and some other amino acids. The aspartic acid and glucosamine were present in equimolar amounts; the aspartic acid was the only amino acid present in an amount equivalent to that of glucosamine. Thus there is the possibility of a linkage between the mannan and the peptide via glucosamine and aspartic acid. 7. Mannose 6-phosphate was shown to be part of the mannan structure. Information about the structure of the mannan and the linkage of the glucosamine was obtained by periodate oxidation studies. 8. The glucosamine present in the glycopeptide could not be released by treatment with an enzyme preparation obtained from the gut of Helix pomatia. This enzyme released glucosamine from the intact cell wall. Thus there are probably at least two polymers containing glucosamine in the cell wall. 9. The biosynthesis of the mannan polymer in the yeast cell wall is discussed with regard to the two types of carbohydrate-amino acid linkages found in the glycoprotein.

show abstract

Section: Discussionsupporting

confidence: 75%

The structure of a glycopeptide isolated from the yeast cell wall

Sentandreu

Northcote

1968

Biochemical Journal

177

View full text Add to dashboard Cite

show abstract

“…The reaction products have chromatographic mob&ties identical to mannobiose., mannotriose, and mannotetraose respectively in solvents A and B. They are completely degraded by emulsin (which contains an exo-cw-mannosidase [4,7]), to yield mannose as the only radioactive product. The mannosyl residues that originate from GDP-14Cmannose are linked as non-reducing termini to the saccharide acceptors according to the following evidence: when the radioactive oligosaccharides are fast reduced with sodium borohydride and then hydrolyzed with 1 N HCl for 3 hr at 100°, mannose is the only radioactive product liberated.…”

Section: Resultsmentioning

confidence: 99%

Biosynthesis of oligosaccharide components of cryptococcus laurentii cell wall

Schutzbach

Ankel

1969

FEBS Letters

View full text Add to dashboard Cite

“…For that reason, reproducibility of the analysis of a water standard was only tested and, using a 1 pmol/L standard solution, the relative standard deviation was found to be 2.6 % (n = 6). 161 …”

Section: Electrophoresismentioning

confidence: 99%

Significant immunological cross‐reactivity of plant glycoproteins

Laine

Faye

1988

Electrophoresis

View full text Add to dashboard Cite

Plant glycoproteins generally cross-react because of the presence of identical or related complex glycans which are highly immunogenic. The use of mild periodate oxidation of glycans after glycoprotein transfer from sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels to nitrocellulose membranes prior to immunodetection is a way of identifying the carbohydrate antigenic determinants of a glycoprotein as the basis for antigenic cross-reaction. Periodate oxidation can distinguish between antibodies directed against carbohydrate and against peptide antigenic determinants, the latter being unaffected by oxidation. Immunoblotting performed after periodate treatment allows the detection of common protein epitopes.

show abstract

Studies on a Glycopeptide From Ovalbumin

Cited by 30 publications

References 28 publications

The structure of a glycopeptide isolated from the yeast cell wall

The structure of a glycopeptide isolated from the yeast cell wall

Biosynthesis of oligosaccharide components of cryptococcus laurentii cell wall

Significant immunological cross‐reactivity of plant glycoproteins

Contact Info

Product

Resources

About