Purification, molecular and enzymic characterization of an acid RNase from the insect Ceratitis capitata.
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.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D006863:Hydrogen-Ion Concentration; D007313:Insecta / Q000201:enzymology*; D008970:Molecular Weight; D011487:Protein Conformation; D012260:Ribonucleases / Q000032:analysis* / Q000302:isolation & purification; D013057:Spectrum Analysis
D000596:Amino Acids; D012260:Ribonucleases