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Prolidases I and II were highly purified from human erythrocytes. The effects of various amino acids, MnCl 2  and mercaptoethanol, on these two enzymes were investigated. Normal prolidase II was very labile in the absence of MnCl 2  or mercaptoethanol. The activity of prolidase II was maintained at about 76% by preincubation with MnCl 2 ; it was then activated up to 140% by treatment with mercaptoethanol for 60 minutes at 37 °C. Normal prolidases I and II showed the highest activity against glycylproline or methionylproline in the presence of MnCl 2 . The activity of prolidase I against glycylproline was enhanced strongly by glycine and MnCl 2 , but not activated in the absence of MnCl 2 . The activity of prolidase II against methionylproline was enhanced three-fold in the presence of glycine and MnCl 2 , but its activity against glycylproline was very low even in the presence of MnCl 2 . A stronger enhancement of this activity was found in normal erythrocytes, and a lower level of this activity was found in erythrocytes of patients treated with glycine, MnCl 2  and mercaptoethanol compared to those treated with glycine and MnCl2. The activity of prolidase II against methionylproline in all erythrocytes, of normal humans and of patients, was strongly activated by the addition of glycine with MnCl 2  but suppressed by the addition of mercaptoethanol. Clin Chem Lab Med 2003; 41(10):13231328

Characteristics of Prolidase from the Erythrocytes of Normal Humans and Patients with Prolidase Deficiency and Their Mother