SUMMARY: A pseudomonad bacterium contaminating a preparation of purified tobacco rattle virus was isolated. It produced proteolytic enzyme activity in nutrient broth + 1 % glucose; activity was greatest in the stationary phase of growth. This enzyme acted on the protein in particles of tobacco rattle virus to produce a polypeptide that migrated more rapidly in sodium dodecyl sulphate-acrylamide gels than untreated virus coat protein. The estimate of molecular weight of the modified protein was less affected by gel strength than that of the unmodified protein. The enzyme appeared as a single component when analysed by polyacrylamide gel electrophoresis or by gel filtration in Sephadex G-100; its apparent molecular weight was about 45000. Enzyme activity did not require added thiol reagents, but was reversibly inhibited by EDTA.


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