Carbohydrates in protein. 5. Procedures for the isolation of glycopeptides from hen's-egg albumin and their oxidation by periodate

Fletcher, Anthony P.; Marks, G. S.; Marshall, Ruth; Neuberger, A.

doi:10.1042/bj0870265

Cited by 67 publications

(29 citation statements)

References 37 publications

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“…This suggests that 2 moles of D-mannose and 2 moles of acetamido-hexose/mole remain unoxidized by periodate because of inter-unit linkages. Bragg & Hough (1961) and Fletcher, Marks, Marshall & Neuberger (1963) obtained similar results after periodate oxidation of the carbohydrate in ovalbumin.…”

Section: Molar Proportionmentioning

confidence: 67%

“…The estimation of acid released during periodate oxidation of glycopeptides is, however, unsatisfactory. Thus a glycopeptide from y-globulin showed a steady release of acid during periodate oxidation (Rothfus & Smith, 1962;Clamp &Putnam, 1964), andFletcher et al (1963) found a similar result with ovalbumin glyco-eptide. The glycopeptide was expected to release 1 equiv.…”

Section: ;mentioning

confidence: 90%

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Studies on a Glycopeptide From Ovalbumin

Clamp¹,

Hough²

1965

Biochemical Journal

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1. The structure of the carbohydrate component of the glycopeptide isolated from the proteolytic digest of ovalbumin has been investigated by chemical and enzymic methods. 2. The results are consistent with the presence of a single carbohydrate prosthetic group, linked through its reducing end group to the peptide chain. 3. Further, all the 2-amino-2-deoxy-d-glucose units appear to be in the N-acylated form, the phenolic hydroxyl group of tyrosine is free and the omega-carboxyl group of aspartic acid is substituted. 4. The carbohydrate component has a branched-chain structure, the two non-reducing ends being terminated by a d-mannopyranosyl and a 2-acetamido-2-deoxy-d-glucopyranosyl residue respectively. 5. The terminal d-mannopyranosyl unit is probably linked through at least one other d-mannopyranosyl residue to the remainder of the carbohydrate.

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Section: Molar Proportionmentioning

confidence: 67%

Section: ;mentioning

confidence: 90%

Studies on a Glycopeptide From Ovalbumin

Clamp¹,

Hough²

1965

Biochemical Journal

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“…The major glyeopeptide of human Tamm-Horsfall glyeoprotein was purified from the glycoprotein isolated from pooled urine, as detailed elsewhere (1). Egg*albumine glyeopeptide was prepared aeeordb~g to FLE~e~E~ et al (10). Pronase (Sigma) was purified by acetone precipitation (19).…”

Section: Methodsmentioning

confidence: 99%

Studies on benzhydrazone, a specific inhibitor of herpesvirus glycoprotein synthesis. Size distribution of glycopeptides and endo-β-N-acetylglucosaminidase-H treatment

Serafini‐Cessi

Campadelli-Fiume

1981

Archives of Virology

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Benzhydrazone is a bis-amidinohydrazone derivative which specifically hinders the formation of herpes simplex virus (HSV) glycoproteins. In this study we present some structural features of the oligosaccharide chains of herpesvirus glycoproteins synthesized in cells incubated with the inhibitor. Gel filtration analysis of glycopeptides, obtained through exhaustive pronase-digestion of infected cells after a long or a short labeling with 14C-glucosamine, showed that benzhydrazone reduced the appearance of glycopeptides of all the size-classes, including the mannose-rich glycopeptide with an approximate molecular weight of 1500. The same percent of label was released from both untreated and benzhydrazone-treated cells after digestion with endo-beta-N-acetylglucosaminidase H, an enzyme which cleaves between the N-acetylglucosamine residues in large high-mannose type oligosaccharides. This indicates that the relative amount of glycoproteins sensitive to this enzyme did not differ in the two kinds of samples. PAGE analysis confirmed that the same glycoproteins were digested in both samples. They were gA, pgC, and pgD, which therefore contain high-mannose type oligosaccharides. It is concluded that benzhydrazone hinders carbohydrate addition to herpesvirus proteins at an early step.

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“…In such a glycopeptide, the aspartic acid is linked directly to N-acetylglucosamine in the form of 1-L-,3-aspartamido(2-acetarnido)-1,2-dideoxy-,l-D-glucose. Such a carbohydrate-protein linkage was first identified in ovalbumin (21,22), and it appears now to occur in many animal proteins (23). Its presence in plant glycoproteins was first described in soybean hemagglutinin (24) and more recently in bromelain and other plant glycoproteins (25).…”

Section: Resultsmentioning

confidence: 99%

Extensive homology between the subunits of the phytohemagglutinin mitogenic proteins derived from Phaseolus vulgaris.

Miller¹,

Hsu²,

Heinrikson³

et al. 1975

Proc. Natl. Acad. Sci. U.S.A.

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The phytohemagglutinin mitogenic proteins derived from Phaseolus vulgaris comprise a class of five glycoproteins that are isomeric tetramers composed of varying proportions of two different subunits (L and R). Within the native tetramer, the L subunit is a potent leukoagglutinin and mitogen that lacks hemagglutinating properties, whereas the R subunit is a potent hemagglutinin with little or no mitogenic activity. The subunits have been isolated in homogeneous form by isoelectric focusing in 8 M urea. Previous work has shown that they have equal molecular weights and differ in amino-acid sequence from residues 1-7, but are identical in positions 8-24 [(1973) J. Exp. Med. 138, 939-9511. We now report amino-acid composition studies which reveal striking similarities between the subunits. Both lack methionine and cysteine. The twelfth residue in each subunit is a glycosylated asparagine, with the identical carbohydrate composition in each. The last three residues of the subunits, as determined by carboxypeptidase A digestion, are identical. Tryptic peptide mapping of the succinylated phytohemagglutinin subunits reveals a high degree of similarity. We conclude that the substantial difference in biological properties among the tetrameric phytohemagglutinin mitogens is a result of relatively restricted differences in the primary structure of their constituent subunits.The phytohemagglutinin (PHAP) mitogenic proteins derived from the red kidney bean, Phaseolus vulgaris, have been shown to comprise a family of five heterogeneous proteins (1, 2). They consist of isomeric, noncovalently bound tetramers which are made up of two different subunits, designated as L and R ( Fig. 1) (2-4). One of the five proteins is a potent leukoagglutinin with low hemagglutinating activity (L-PHAP); it is homogeneous, consisting of four identical subunits (1). Three other, closely related proteins, which have modest leukoagglutinating but potent hemagglutinating properties (H-PHAP), have also been isolated. They consist of hybrid tetramers containing varying proportions of the two subunits (2-2R, 1L3R, and 4R), the increasing R subunit content of which is reflected by increasingly cathodal migration on polyacrylamide gel electrophoresis. A fifth PHAP mitogenic protein (3L-1R) has been identified, but detailed study of its properties has been hampered in the past by its contamination with other proteins. We have tentatively concluded that, within each native tetramer, the L subunit has strong mitogenic activity and a high affinity for receptors of lymphocyte membranes, but little or no affinity for those of erythrocytes.Conversely, the R subunit has a high affinity for erythrocyte membrane receptors, but little for those of lymphocytes. As a result, the 4R tetramer displays little or no lymphocyte mitogenic activity (6). The hybrid molecules (1L-3R, 2L-2R, and 3L-1R tetramers) have been found to be mitogenic, to cause mixed agglutination of erythrocytes and lymphocytes, and to have enhanced lymphocyte-transforming capability in the p...

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Carbohydrates in protein. 5. Procedures for the isolation of glycopeptides from hen's-egg albumin and their oxidation by periodate

Cited by 67 publications

References 37 publications

Studies on a Glycopeptide From Ovalbumin

Studies on a Glycopeptide From Ovalbumin

Studies on benzhydrazone, a specific inhibitor of herpesvirus glycoprotein synthesis. Size distribution of glycopeptides and endo-β-N-acetylglucosaminidase-H treatment

Extensive homology between the subunits of the phytohemagglutinin mitogenic proteins derived from Phaseolus vulgaris.

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