Abstract
An acid ribonuclease has been purified from the insect Ceratitis capitata. The specific activity of the purified enzyme is 580 units/mg. This enzyme is a single polypeptide chain of about 35.5 kDa, containing only one disulfide bridge and no free -SH groups. The A0.1%1cm at 280 nm is 1.90. The hydrodynamic radius of the native enzyme is 2.5 nm. The secondary structure of this RNase is composed of 10% alpha-helix, 31% beta-structure and 59% aperiodic conformation with an average number of residues per helical segment of 10, based on circular dichroic measurements. Optimum parameters for the enzyme activity are pH 5.5, 0.15 M ionic strength and 40 degrees C. Divalent cations are not required for the enzymic catalysis. This enzyme has been characterized as cyclizing endoribonuclease.
Published Version
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