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.
Fritz
M A
MA
Department of Molecular Genetics and Microbiology, University of Medicine and Dentistry of New Jersey, School of Osteopathic Medicine, Piscataway 08854.
Fallon
A M
AM
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