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Chloroperoxidase

I. ISOLATION AND PROPERTIES OF THE CRYSTALLINE GLYCOPROTEIN

From the ¹ From the Biochemistry Division, Department of Chemistry and Chemical Engineering, University of Illinois, Urbana, Illinois 61803

Chloroperoxidase from Caldariomyces fumago has been isolated in crystalline form. The prosthetic group of chloroperoxidase is ferriprotoporphyrin IX. On the basis of the heme content, the minimal molecular weight of chloroperoxidase is 40,200. On the basis of hydrodynamic measurements, the molecular weight of chloroperoxidase is approximately 42,000. Therefore, in solution at neutral pH, chloroperoxidase behaves as a monomeric species.

The spectral properties of the oxidized and reduced forms of the enzyme and also of the azide and cyanide complexes are reported.

The amino acid composition of chloroperoxidase is reported. Chloroperoxidase is rich in aspartic acid, glutamic acid, and serine and proline residues. These four amino acids constitute 45% of the total amino acid content.

Chloroperoxidase is a glycoprotein. Approximately 25 to 30% of the molecule is carbohydrate. Chromatography of acid hydrolysates reveals that glucosamine and arabinose are major constituents.

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