The inactivation of a bacteriophage by a component of papain

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Abstract
A bacteriophage, phage 3, originally isolated from Oxford sewage, is inactivated by dilute extracts of papain. The inactivation is blocked by cysteine, citrate and ethylenediaminetetra-acetic acid, which suggests that a metal might be involved in the system. The protease of papain, when crystallized by the procedure of Kimmel and Smith (1954), was found to possess thiolesterase activity as shown by Johnston (1956). The thiolesterase has no effect on phage 3 although Kozloff et al. (1957) have found that the somewhat similar phages T2 and T4 are inactivated by the thiolesterase of crystalline papain. The antiphage component of crude papain has been separated by zone electrophoresis and found to have no thiolesterase activity.