Enzyme activity and bacteriophage infection. II. Activities before and after virus infection

A B PARDEE, R E KUNKEE
1952 Journal of Biological Chemistry  
In studying the mechanism of bacteriophage infection, changes in the various enzyme activities of the bacteria during lysis are of interest. Any definite variations in activities might provide an insight to processes occurring during virus multiplication. In this paper are presented studies of activities before and after virus infection of nine bacterial enzymes: apyrase, pyruvic oxidase, formic dehydrogenase, serine deaminase, ribonuclease, desoxyribonuclease, two proteases, and catalase. The
more » ... and catalase. The choice of enzymes to be assayed in the lysates was designed to give a broad scope to the survey. Restriction of the study to several enzymes all of one "classification," for example, enzymes of carbohydrate metabolism, would produce little information if the results showed no deviation of these activities from the normal. If a broad variety of enzymes is studied and the results show no deviation due to infection, they indicate little change in many types of metabolism. Still, this does not mean that there are no enzymatic disturbances during infection, but may only mean that the survey was not large enough. The literature contains no surveys of enzyme activities of bacteria lyzed by bacteriophage, probably because of the difficulty of preparing lysates which show any enzymatic activity. Sevag et al. (1) remark that "no clear-cut evidence of metabolic activity of either purified phage preparations or concentrated lyzates has as yet been demonstrated." Cohen in a review (2) cites high activities of protease and desoxyribonuclease found in Escherichiu c& lyzed by T2r+ bacteriophage, but no details are given. In order to obtain lysates with demonstrable enzyme activity, it is necessary to make a much more concentrated preparation than is normally used in bacteriophage work. Therefore, a preliminary problem is to develop a method of preparation of concentrated lysates and yet avoid, as far as possible, inactivation of enzymes and dilution or destruction of cofactors. Interpretation of the enzyme activities of lysates depends upon comparison with activities of extracts produced by other means. Lominski (3) and Kagan (4) were able to show catalase activity in bacterial lysates, but neither of these workers compared the activities with catalase activ-9 by guest on March 23, 2020 http://www.jbc.org/ Downloaded from
pmid:12999811 fatcat:twjb35zvzjewdivb3hfonrzdty