Properties of a ribonuclease from Aedes aegypti larvae.
1. The properties of a soluble ribonuclease from Aedes aegypti larvae have been compared with ribonuclease activity in adult female tissue. 2. In larval extracts ribonuclease activity was maximal at 40-45 degrees C whereas activity in tissue from adult females was highest at 50 degrees C. 3. Ribonuclease activity that was recovered in a 20-60% ammonium sulfate precipitate was further purified by batch elution from DEAE-Sephacel and from carboxymethylcellulose. 4. Ribonuclease activity in the partially purified fraction was sensitive to EDTA, stimulated by magnesium, had a pH optimum at 9.0 and a Mr of 45,000. 5. Agarose gels containing yeast RNA substrate were used to monitor partial purification of the larval ribonuclease.
Department of Molecular Genetics and Microbiology, University of Medicine and Dentistry of New Jersey, School of Osteopathic Medicine, Piscataway 08854.
M A
MA
Fritz
A M
AM
Fallon
D000330:Aedes / Q000201:enzymology* / Q000254:growth & development; D000818:Animals; D011232:Chemical Precipitation; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D006358:Hot Temperature; D007814:Larva / Q000201:enzymology; D012260:Ribonucleases / Q000302:isolation & purification*
D012260:Ribonucleases