Inhibition of wall autolysis of staphylococci by sodium polyanethole sulfonate “liquoid”

Summary Liquoid (polyanethole sulfonate) was neither capable of influencing the growth nor the viability of staphylococci. But liquoid induced a suppression of the activity of different autolytic wall systems of normally growing staphylococci, i.e., autolysins which participate in cross wall separation as well as autolysins which are responsible for cell wall turnover. Additionally, the lysostaphin-induced wall disintegration of staphylococci was inhibited by liquoid.However, no indication could be found for a direct inhibition of lytic wall enzymes by liquoid; rather an interaction of liquoid with the target structure for the autolytic wall enzymes, the cell wall itself, was postulated. On the basis of the experimental data with the teichoic acid^- mutant S. aureus 52A5 the sites of wall teichoic acid were supposed to be an important target for the binding of liquoid to the staphylococcal cell wall.     

Effect of Myxovirus Infection on Synthesis of Cellular Ribonucleic Acid

Ribonucleic acid (RNA) synthesis of chick embryo fibroblasts was inhibited by two members of the myxovirus group, Newcastle disease virus (NDV) and fowl plague virus. It was also found that cellular deoxyribonucleic acid-dependent RNA polymerase was inhibited by a cytoplasmic factor induced by NDV infection.     

Beef liver esterase. II. Kinetic properties

The kinetic parameters, k_cat and K_M, in beef liver esterase-catalyzed hydrolysis were determined for about 100 substrates, which can be classified in several groups: (1) In the ethyl ester series of fatty acids K_M decreases with elongation of the acid, while k_cat has a maximum value with pentanoate. (2) Alkyl acetates are better substrates as the alkyl moiety is longer, whereas esters with branched alkyl groups become worse substrates. (3) Aryl esters are very good substrates. (4) Esters of dicarboxylic acids are good substrates, but only one ester group is cleaved by the enzyme. Fumarate diester is susceptible to esterase hydrolysis, while maleate is not. (5) Esters of hydrophobic amino acids are very good substrates; the enzyme is not stereoselective and both the l and d stereoisomers are readily hydrolyzed. Branching at the β-carbon atom leads to loss of activity, and blocking of the amino group abolishes it. Fluoride ion and dl-malate esters are potent competitive inhibitors of the enzymic reaction. The optimal pH was found to lie between 8 and 8.5. The reaction rate increased between 5 and 40 °C then dropped sharply. The activity decreased at high salt concentration.