Some properties of Aplysia myoglobin covalently bound to a solid matrix

Abstract

A covalent binding of Aplysia myoglobin to an insoluble polysaccaride matrix (Sephadex) was obtained using cyanogen bromide as an activating agent for the oxidrilic groups of the resin. A qualitative comparison has been made between some of the structural and functional properties of the protein in solution and in the bound state. The absorption spectra in the Soret region of the protein-matrix complex differ very slightly from those in the solution state. Aplysia myoglobin can exist in solution in two conformational states (native and denatured) which the protein can reversibly assume depending on conditions of temperature and solvent composition. The protein can be coupled to the solid matrix in both states by changing the conditions in which the coupling process is made to occur. The two conformational states of the protein are stabilized, although to a different extent, by the covalent binding to the resin. Thus, it has been possible to compare the properties of the two states under the same conditions of temperature and solvent compositions.