Glycoprotein biosynthesis: Purification and characterization of a glycoprotein: Galactosyl transferase from Ehrlich ascites tumor cell membranes

Caccam, Juanita F.; Eylar, E.H.

doi:10.1016/0003-9861(70)90445-5

Cited by 30 publications

(4 citation statements)

References 17 publications

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“…1 and 2). These values are in good agreement with those obtained for other galactosyltransferases (Kim et al, 1972;Caccam & Eylar, 1970). All the radioactivity incorporated into fetuin acceptor by the enzyme co-chromatographed with genuine galactose in two solvent systems (A and B).…”

Section: Amino Acidsupporting

confidence: 90%

Role of cell membrane galactosyltransferase in concanavalin A agglutination of erythrocytes

Podolsky

Weiser

1975

Biochemical Journal

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It has been previously observed that rabbit erythrocyte cell surface galactosyltransferase appears to play a role in concanavalin A agglutination of these erythrocytes (Podolsky et al., 1974). Further, a correlation between the occurrence or level of cell surface galactosyltransferase and concanavalin A agglutinability of other cell types has also been observed. The mechanism by which rabbit erythrocyte galactosyltransferase participates in concanavalin A agglutination has now been further defined. The enzyme was solubilized and purified. Characterization of the enzyme properties has shown them to be similar to those reported for other purified galactosyltransferases. Amino acid and carbohydrate analysis showed a high asparagine content and the presence of D-mannose. Specific alpha-mannosidase treatment of the enzyme showed that some of these D-mannose residues were terminal sugars. The purified enzyme also conferred concanavalin A agglutinability to non-agglutinable human erythrocytes. However, the ability to confer concanavalin A agglutinability was unrelated to the enzyme activity per se (as measured with fetuin acceptor) but appeared to be entirely dependent on the presence of terminal alpha-linked D-mannosyl residues in the enzyme structure. These findings suggest that the presence of terminal alpha-mannosidyl residues on cell surface glycoproteins such as galactosyltransferase may be the determining factor in agglutination of cells by concanavalin A.

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Section: Amino Acidsupporting

confidence: 90%

Role of cell membrane galactosyltransferase in concanavalin A agglutination of erythrocytes

Podolsky

Weiser

1975

Biochemical Journal

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“…The properties ofthe glycosyltransferases examined were similar to those described by Caccam & Eylar (1970) and…”

Section: Glycoprotein Galactosyltransferasesupporting

confidence: 75%

“…Assay ofenzymic activities UDP-galactose-glycoprotein galactosyltransferase activity (glycoprotein galactosyltransferase; EC 2.4.1.38) was assayed by the method of Caccam & Eylar (1970) and UDP-N-acetylgalactosamine-polypeptide N-acetylgalactosaminyltransferase activity (polypeptide N-acetylgalactosaminyltransferase) was assayed by the method of . The radioactive products were counted on glassfibre squares in toluene-based scintillant (Stoddart & Northcote, 1967).…”

Section: Electron Microscopymentioning

confidence: 99%

Isolation of a Golgi-apparatus-enriched fraction from leukaemic cells

Warley¹,

Cook²

1976

Biochemical Journal

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1. A Golgi-apparatus-enriched fraction was isolated from acute leukaemic lymphoblasts of AKR mice by using an homogenate stabilized with 1 mM-glutaraldehyde. 2. The isolated fraction, which was shown morphologically to be enriched in dictyosomes, possessed between 44- and 76-fold increase in specific activity, compared with the tumour homogenate, of UDP-galactose-glycoprotein galactosyltransferase and between 3- and10.5-fold increase in relative specific activity of UDP-N-acetygalactosamine-polypeptide N-acetylgalactosaminyltransferase. 3. Plasma membranes isolated from the leukaemic lymphoblasts also possessed glycoprotein galactosyltransferase activity, though in contrast with Golgi-apparatus-enriched material had no detectable polypeptide N-acetygalactosaminyltransferase. 4. The difficulties associated with maintaining the morphological integrity of the Golgi apparatus in subcellular fractionation are discussed.

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“…The galactosyl transferase from human milk resembles several other glycosyl transferases in having maximum activity at a lower temperature than is usual for enzymes. For example, maximum activity at 24 ° was reported for a galactosyl transferase from Ehrlich ascites tumour cell membranes [8] and at 22 °, 28 ° and 37 ° for particlebound galactosyl, N-acetylglucosaminyl and mannosyl transferases, respectively, from epithelial cells of rat Small intestine [9]. A sialyl transferase found in soluble form in human serum and in membrane-bound form in the erythrocytes had maximum activity at 37 ° in both instances [10], suggesting that the temperature optimum is a characteristic of the enzyme itself rather than of the form in which it occurs.…”

Section: Discussionmentioning

confidence: 99%

The effect of temperature on a reaction catalysed by lactose synthetaseA protein

Kitchen¹,

Andrews²

1972

FEBS Letters

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Glycoprotein biosynthesis: Purification and characterization of a glycoprotein: Galactosyl transferase from Ehrlich ascites tumor cell membranes

Cited by 30 publications

References 17 publications

Role of cell membrane galactosyltransferase in concanavalin A agglutination of erythrocytes

Role of cell membrane galactosyltransferase in concanavalin A agglutination of erythrocytes

Isolation of a Golgi-apparatus-enriched fraction from leukaemic cells

The effect of temperature on a reaction catalysed by lactose synthetaseA protein

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