Polyphenol oxidases (PPO) are copper metaloproteins that catalyse the oxidation of o-diphenols to quinones, highly reactive molecules which readily bind to nucleophilic sites on cellular components and proteins. Red clover protein, due to this enzyme is resistant to protease degradation during. Theses enzymes (circa. 60-65 kDa) are located in the thylakoid lumen and can be converted to a 40-45 kDa form by proteolysis both in vitro and in vivo (Gelder et al., 1997). Conversion to the smaller form has been demonstrated to confer activity at neutral pH. Other treatments, such as the presence of lipids or detergents eg. SDS, can also confer activity at pH7 (Gelder et al., 1997). Here we describe studies on treatments that affect red clover PPO activity at neutral pH, which is equivalent to the physiological pH of macerated/homogenised leaf extracts