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Occurrence and Consequence of Superoxide Dismutase in Milk Products¹: A Review

Animal Sciences Department, University of Kentucky, Lexington 40546

ABSTRACT

Introduction

The biological function of the protein erythrocuprein was discovered by McCord and Fridovich (23) in 1969 while examining the reduction of cytochrome c by xanthine oxidase. McCord and Fridovich (23) suggested the name superoxide dismutase (SOD) for erythrocuprein, because it catalyzed the enzymic dismutation of superoxide anions (O₂). Superoxide dismutase is an enzyme ubiquitous to microbial, plant, and animal systems. Essentially three families of SOD have been observed in various tissues. Animals have two metallo-enzymes that are capable of dismutating O₂. The most abundant enzyme is the Cu/Zn enzyme that was isolated first from blood (24). This blue-green enzyme consists of two similar polypeptides having two atoms each of Zn and Cu (4), and it has a molecular weight of approximately 32,000 (24). Mitochondria and liver contain an Mn-containing enzyme (31) which comprises approximately 8% of the total animal SOD (24). The pink-colored, Mn enzyme is a tetramer with a molecular weight of 80,000 (31).

¹ This manuscript (79-5-143) is published with the approval of the Director of the Kentucky Agriculture Experiment Station.

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