Selective solubilization by melittin of glycophorin A and acetylcholinesterase from human erythrocyte ghosts.

Melittin, the main basic and hydrophobic peptide of bee venom, has been used for solubilizing membrane components of the human erythrocyte ghost. Up to 1.0 mM, it does not extract any phospholipid.

Receptor-like activity of a monoclonal anti-idiotypic antibody against an anti-acetylcholine receptor antibody.

A monoclonal anti-idiotypic antibody against an anti-acetylcholine receptor antibody from a patient with myasthenia gravis was shown to bind the cholinergic ligand alpha-bungarotoxin. This binding could be inhibited by other cholinergic ligands, both antagonists and agonists. The anti-idiotype was also able to elicit the production of anti-receptor antibodies in mice.

Lack of cross-reactivity of a monoclonal antibody against the neurotransmitter site of Torpedo nicotinic acetylcholine receptor with muscle receptors from several sources.

A monoclonal antibody raised against Torpedo nicotinic acetylcholine receptor has been used to study the neurotransmitter binding site of the acetylcholine receptor from several sources. When tested on Torpedo receptor, this monoclonal antibody inhibited binding of alpha-bungarotoxin to 50% of the available sites. The failure to completely inhibit binding of the toxin is attributed to the orientation of the determinant for the monoclonal antibody on the receptor molecule.

Evidence for sialic acid on the nicotinic acetylcholine receptor from Torpedo marmorata.

The nicotinic acetylcholine receptor from Torpedo marmorata was treated with neuraminidase. Direct determination of sialic acid released gave about 1 mole sialic acid per mole receptor. Lectin binding studies of the sugars accessible on the receptor molecule were performed after sialic acid hydrolysis.