Abstract
We have purified from T4 phage-infected cells an enzyme which cleaves purified prehead proteins to the size found in mature virions. Its specificity corresponds to that found in vivo since its action results in the creation of a new alanine amino-terminal on cleaved IPIII. We call this enzyme T4 prehead proteinase (T4PPase), because it acts on the proteins of the precursor to the T4 capsid. However, in vitro, the precursor proteins need not be assembled into a structure to be substrates for the enzyme. T4PPase requires neither an active serine nor a sulfhydryl group for activity. It is rapidly inactivated by autodigestion.
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