Affinity chromatography on Con A‐Sepharose of synaptic vesicle membrane glycoproteins

Zanetta, Jean‐Pierre; Gombos, G.

doi:10.1016/0014-5793(74)81029-x

Cited by 16 publications

(2 citation statements)

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“…Concanavalin A (Con A)-binding glycoproteins (for review, see Brunngraber, 1979) in brain tissue include the acetylcholine (nicotinic) receptor (Seto et al, 1977;Moore and Brady, 1977), adenylate cyclase (Michaelis and Michaelis, 1976), thromboplastin (Pitlick, 1976), alkaline phosphatase (Chang et al, 1975), a2-brain-specific glycoprotein , dopamine-p-hydroxylase (Aunis et al, 1979, glutamate-binding protein (Michaelis, 1975), glycoprotein GM-50-C (Ramirez et al, 1974), phosphoglycoproteins (Davis et al, 1976), sulfatases and all glycosidases (Balasubramanian and Bachhawat, 1975), and acetylcholinesterase (Rieger and Vigny, 1976). Membranous fractions shown to bind Con A include components of the chromaffin granules (Eagles et al, 1975), Golgi membranes (Abe et al, 1976), myelin (Matus et al, 1973), nuclear membrane (Virtanen and Wariouaara, 1976), ribosomal protein (Howard and Schnebli, 1977), smooth endoplasmic reticulum (Wood and McLaughlin, 1976a), synaptosomes (Matus et al, 1973;Matus and Walters, 1976), synaptic plasma membranes (Zanetta et al, 1975), postsynaptic densities (Gurd, 1977), synaptic junctions (Kelly and Cotman, 1977), proteins of the synaptic cleft (Collard and Temmink, 1974;Wood and McLaughlin, 19766), and synaptic vesicles (Zanetta and Gombos, 1974).…”

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Structure of the Mannose‐Rich Oligosaccharide Chains of Concanavalin A‐Binding Glycopeptides Derived from Beef Brain Glycoproteins

Somawardhana

Brunngraber

1983

Journal of Neurochemistry

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A neutral, mannose-rich, concanavalin A (Con A)-binding glycopeptide fraction was obtained by proteolytic digestion of defatted beef brain tissue. Hydrazinolysis followed by gel filtration of the reaction products provided three oligosaccharides. A portion of each oligosaccharide was treated by exhaustive digestion with alpha-mannosidase. Another portion was subjected to selective acetolysis of Man alpha 1 leads to 6Man linkages, providing two fragments that were recovered by gel filtration. The structure of the intact oligosaccharides, as well as the fragments obtained by selective acetolysis and enzymatic treatment, were resolved by gas-liquid chromatographic-mass spectrometric analysis. The structures of the three oligosaccharides were: (a) Man alpha 1 leads to 2Man alpha 1 leads to 6(Man alpha 1 leads to 3)Man alpha 1 leads to 6(Man alpha 1 leads to 2Man alpha 1 leads to 2Man alpha 1 leads to 3)Man beta 1 leads to 4-N-acetylglucosamine (GlcNAc)beta 1 leads to 4N-acetylglucosaminitol (GlcOLNAc); (b) Man alpha 1 leads to 2Man alpha 1 leads to 6(Man alpha 1 leads to 3)Man alpha 1 leads to 6(Man alpha 1 leads to 2Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcOLNAc; and (c) Man alpha 1 leads to 6(Man alpha 1 leads to 3) Man alpha 1 leads to 6(Man alpha 1 leads to 3)Man beta 1 leads to 4GlcNAc-beta 1 leads to 4GlcOLNAc. These structures account for 15-20% of the glycoprotein-carbohydrate of whole beef brain and most of the oligosaccharides that demonstrate a high affinity for Con A. In view of the large number of Con A-binding glycoproteins in brain tissue, it appears that many of these different glycoproteins must contain structurally identical oligosaccharides.

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confidence: 99%

Structure of the Mannose‐Rich Oligosaccharide Chains of Concanavalin A‐Binding Glycopeptides Derived from Beef Brain Glycoproteins

Somawardhana

Brunngraber

1983

Journal of Neurochemistry

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“…ZANETTA et al., 1977) while the proteins of nervous system membranes other than myelin are virtually all insoluble in chloroform-methanol (ADAMS, 1972;ZANETTA & GOMBOS, 1974;ZANEITA et al, 1975).…”

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Minor proteins of CNS myelin fractions: are they intrinsic to the myelin sheath?

1977

Journal of Neurochemistry

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A 33 kDa protein band in enhanced during long‐term adaptation of EUE cells to a hypertonic medium

Giuliani

Ferraretto

Conti

et al. 1991

Cell Biochemistry & Function

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A cell line derived from human embryonic epithelium (EUE cells) shows an enhanced expression of a 33 kDa protein when adapted to grow in a hypertonic medium containing 0.246 M NaCl (1.8 x the isotonic concentration). The maximum amount of this protein, followed by SDS-PAGE electrophoresis, was found after 4 days of adaptation; thereafter, the protein band remained fairly constant up to 30 days. When the cells were transferred back to a medium containing 0.137 M NaCl (isotonic medium), the protein pattern reverted to that of control cells. This protein is mainly localized in the cytosol, although a small part is associated with the 150,000 g pellet and needs detergents to be extracted. The molecular weight and the cellular location suggest a possible analogy with the so-called amphitropic proteins, that are known to interact with both the epidermal growth factor receptor and hydrophobic structures, such as the membrane phospholipids and the cytoskeletal components.

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Affinity chromatography on Con A‐Sepharose of synaptic vesicle membrane glycoproteins

Cited by 16 publications

References 9 publications

Structure of the Mannose‐Rich Oligosaccharide Chains of Concanavalin A‐Binding Glycopeptides Derived from Beef Brain Glycoproteins

Structure of the Mannose‐Rich Oligosaccharide Chains of Concanavalin A‐Binding Glycopeptides Derived from Beef Brain Glycoproteins

Minor proteins of CNS myelin fractions: are they intrinsic to the myelin sheath?

A 33 kDa protein band in enhanced during long‐term adaptation of EUE cells to a hypertonic medium

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