PMID: 1185594Nov 1, 1975Paper

Binding of d-tubocurarine di (methyl-14C) ether iodide and other amines to cartilage, chondroitin sulfate and human plasma proteins.

The Journal of Pharmacology and Experimental Therapeutics
G D OlsenW K Riker

Abstract

The binding of d-tubocurarine di [methyl-14C] ether iodide (d-TCE) and other amines to bovine nasal septum, chondroitin sulfate (CS) and human plasma proteins was examined by equilibrium dialysis. Bovine nasal septum and CS bound d-TCE to a greater extent than they did morphine, d-methadone (d-ME) and l-methadone (l-ME). Cartilage, relative to an equal weight of pure CS, bound slightly more d-TCE, 50% more d-ME and l-ME, and the same amount of morphine. The amount of d-TCE bound to pure CS was similar to that of decamethonium [methyl-14C] dibromide but less than that of two new iodinated bisquaternary compounds: 1,6-bis(N,N-dimethyl-3-iodobenzylamino)hexane dichloride and 1,6-bis[dimethyl-(3-amino-4,6-diiodo-benzyl)amino]hexane dichloride. The binding of d-TCE is greater for pure CS than for impure CS which contains 26% protein, and binding to either preparation was inversely related to sodium ion concentration. In the drug concentration range explored, 30 to 40% of d-TCE is bound to plasma proteins, which is twice that of decamethonium binding but equivalent to the binding of morphine and about one-half the binding of d-ME and l-ME. In this same drug concentration range, each gram of cartilage (dry weight) can bind about 10(-7...Continue Reading

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