SOME OBSERVATIONS ON THE „LATENT” RIBONUCLEASE OF ESCHERICHIA COLI

Abstract

Most of the so-called "latent" ribonuclease of E. coli can be released from spheroplasts in 5 min. although the spheroplast ribosomes remain intact as demonstrated by RNA content, sucrose-density gradient profiles and ability to adsorb soluble RNase. Ribosomes adsorb up to a 12-fold excess of soluble RNase even under dissociated conditions. All of the RNase binds to 30s particles. Spheroplasts prepared by lysozyme alone release neither alkaline phosphatase nor RNase, but nearly half of the alkaline phos-phatase can be removed by washing EDTA-treated E. coli, although other enzymes are not released.