Molecular Sieve Studies of Interacting Protein Systems
نویسنده
چکیده
Highly purified preparations of D-aIIIiII0 acid oxidase were obtained by removal of high molecular weight components after purification by established procedures. Molecular sieve studies were carried out on the size characterization of the highly purified apoenzyme molecule. In the microgram per ml concentration range the apoenzyme was shown to dissociate to a subunit with a molecular Stokes radius of 25.1 f 1 A and a molecular weight of 35,000 to 40,000. This molecular weight corresponds to that of a single flavin adenine dinucleotide-binding unit and presents the possibility that the monomer of the holoenzyme may be the active species.
منابع مشابه
Molecular Sieve Studies of Interacting Protein Systems
Studies of chemically reacting systems of macromolecules by conventional transport experiments are subject to inherent ambiguities. These uncertainties often prohibit an unequivocal determination of the explicit reactions which give rise to the average propexties being measured. Such difficulties may be circumvented with molecular sieve chromatography in which subunit dissociation curves are ob...
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