TY - JOUR
T1 - Properties of a ribonuclease from Aedes aegypti larvae
AU - Fritz, Mary Ann
AU - Fallon, Ann Marie
PY - 1987
Y1 - 1987
N2 - 1. 1. The properties of a soluble ribonuclease from Aedes aegypti larvae have been compared with ribonuclease activity in adult female tissue. 2. 2. In larval extracts ribonuclease activity was maximal at 40-45°C whereas activity in tissue from adult females was highest at 50°C. 3. 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. 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. 5. Agarose gels containing yeast RNA substrate were used to monitor partial purification of the larval ribonuclease.
AB - 1. 1. The properties of a soluble ribonuclease from Aedes aegypti larvae have been compared with ribonuclease activity in adult female tissue. 2. 2. In larval extracts ribonuclease activity was maximal at 40-45°C whereas activity in tissue from adult females was highest at 50°C. 3. 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. 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. 5. Agarose gels containing yeast RNA substrate were used to monitor partial purification of the larval ribonuclease.
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U2 - 10.1016/0305-0491(87)90350-6
DO - 10.1016/0305-0491(87)90350-6
M3 - Article
C2 - 3427905
AN - SCOPUS:0023495351
VL - 88
SP - 595
EP - 601
JO - Comparative Biochemistry and Physiology -- Part B: Biochemistry and
JF - Comparative Biochemistry and Physiology -- Part B: Biochemistry and
SN - 0305-0491
IS - 2
ER -