Open AccessMonomerization of cytochrome oxidase may be essential for the removal of subunit III
Author(s) -
FINEL Moshe,
WIKSTRÖM Mårten
Publication year - 1988
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1988.tb14259.x
Subject(s) - protein subunit , chemistry , cytochrome c oxidase , biochemistry , dimer , enzyme , fast protein liquid chromatography , oxidase test , cytochrome , organic chemistry , gene
1 Incubation of cytochrome oxidase, under conditionsused as intial steps in treatment to remove sub‐unit III, causes at least partial monomerization of the enzyme. 2 The extent of removal of subunit III by anion‐exchange fast protein liquid chromatography (FPLC) is much increased if the enzyme is fully monomerized before it is applied to the column. 3 Subunit III is incompletely removed by chymotrypsin treatment. A digestion product of subunit III migrating in SDS‐PAGE like subunit IV, is detected with specific antibodies. The amount of this product is reduced when monomerization is increased by raising the detergent/protein ration. 4 The results suggest that monomerization facilities removal of subunit III and exposes it to further chymotrypsin digestion. We propose that subunit III is at least in part located in the junction between the monoments in the cytochrome oxidase dimer.