Properties of a ribonuclease from Aedes aegypti larvae

Mary Ann Fritz; Ann Marie Fallon

doi:10.1016/0305-0491(87)90350-6

Properties of a ribonuclease from Aedes aegypti larvae

Mary Ann Fritz
, Ann Marie Fallon

Entomology

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

Abstract

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 M_r of 45,000. 5. 5. Agarose gels containing yeast RNA substrate were used to monitor partial purification of the larval ribonuclease.

Original language	English (US)
Pages (from-to)	595-601
Number of pages	7
Journal	Comparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume	88
Issue number	2
DOIs	https://doi.org/10.1016/0305-0491(87)90350-6
State	Published - 1987

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title = "Properties of a ribonuclease from Aedes aegypti larvae",

abstract = "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.",

author = "Fritz, \{Mary Ann\} and Fallon, \{Ann Marie\}",

year = "1987",

doi = "10.1016/0305-0491(87)90350-6",

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pages = "595--601",

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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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DO - 10.1016/0305-0491(87)90350-6

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AN - SCOPUS:0023495351

SN - 0305-0491

VL - 88

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JO - Comparative Biochemistry and Physiology -- Part B: Biochemistry and

JF - Comparative Biochemistry and Physiology -- Part B: Biochemistry and

IS - 2

ER -

Properties of a ribonuclease from Aedes aegypti larvae

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