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M De Villiers

Publications and source records attributed to M De Villiers.

3 recordsLinked to original sources

A radioimmunoassay for metoclopramide.

A radioimmunoassay for the anti-emetic drug, metoclopramide, in the pmol range was developed. The immunogen was prepared by photolytic coupling of metoclopramide to bovine serum albumin. A crosslinking reagent, N-hydroxy-succinimidyl-4-azidobenzoate, was first reacted with serum albumin through nucleophilic substitution. Ultraviolet irradiation (lambda greater than 300 nm) of the photoactive serum albumin conjugate in the presence of metoclopramide resulted in covalent attachment of the drug to the protein. An 125I-labelled metoclopramide derivative was prepared by diazotisation of the aromatic amine group and substitution of the resultant diazo group with 125I-. Binding data of the antibody with radioiodinated metoclopramide gave a linear Scatchard plot indicative of a homogeneous antibody population. A dissociation constant of 3 X 10(-11) mol/l was calculated for the antigen-antibody interaction. The antibodies showed negligible cross-reactivity with lignocaine which is structurally closely related to metoclopramide.

Albumins

Mitochondrial Ca2+ fluxes: role of free fatty acids, acyl-CoA and acylcarnitine.

It has been suggested that accumulation of lipid metabolites, such as fatty acids, fatty acyl-CoA and acylcarnitine, in the ischaemic myocardium, may be responsible for disturbances in mitochondrial Ca2+ fluxes. In view of the presence of an intracellular fatty acid binding protein, the question arose whether these intermediates affect mitochondrial Ca2+ uptake and release similarly in vivo. In this study the effects of linoleic acid, palmitic acid, palmitoyl-CoA and palmitoylcarnitine were studied on mitochondrial Ca2+ fluxes in the absence and presence of albumin, an avid binder of fatty acid derivatives. Albumin reversed the effects of the above compounds on mitochondrial Ca2+ uptake and release, suggesting that the presence of an intracellular fatty acid binding protein may protect the ischaemic myocardial cell against the deleterious effects of accumulated fatty acid derivatives.

Acyl Coenzyme A