Elsevier

Journal of Insect Physiology

Volume 17, Issue 6, June 1971, Pages 1139-1143, 1145-1151
Journal of Insect Physiology

General esterases of silkmoth moulting fluid: Preliminary characterization

https://doi.org/10.1016/0022-1910(71)90016-3Get rights and content

Abstract

The moulting fluid of silkmoths contains not only proteolytic enzymes with amino acid esterase activity, but also two naphthyl esterases (general esterases). These enzymes have been partially purified and separated by sucrose density-gradient centrifugation and DEAE-cellulose column chromatography. One is weakly anionic at pH 8 and has a molecular weight of 64,000; the other is cationic and has a molecular weight of 57,000. Both enzymes are most stable under the mildly alkaline pH conditions characteristic of moulting fluid but are irreversibly inactivated at acid pH. Both are inhibited by diisopropyl fluorophosphate, although at different rates. The enzymes hydrolyse low molecular weight esters of aromatic alcohols, but lack proteolytic activity; inhibition and specificity studies suggest that they are carboxyl esterases. They are found throughout development, in both moulting gel and moulting fluid; their rôle in the moulting process is as yet unclear.

References (18)

There are more references available in the full text version of this article.

Cited by (34)

  • Oviposition behaviour and biochemical response of an insect pest, Zeugodacus cucurbitae (Coquillett) (Diptera: Tephritidae) to plant phenolic compound phloroglucinol

    2022, Comparative Biochemistry and Physiology Part - C: Toxicology and Pharmacology
    Citation Excerpt :

    The increase in absorbance was measured spectrophotometrically at 340 nm for 5 min at 25 °C. ESTs were extracted and estimated using methodology of Katzenellenbogen and Kafatos (1971). Larval homogenate was prepared in chilled 0.1 M sodium phosphate buffer (pH 6.5).

  • Functional analysis of insect molting fluid proteins on the protection and regulation of ecdysis

    2014, Journal of Biological Chemistry
    Citation Excerpt :

    Approximately 30 μg of cell lysates or 30 μg of molting fluid were loaded on each lane for native gel separation. Methods to detect superoxide dismutase (14), catalase (15), protease (16), and esterase (17) activities in a native gel were performed as described previously. To detect PO activity in molting fluids, each type of molting fluid (10 μg) was added directly to 100 μl of dopamine solution (10 mm dopamine dissolved in 10 mm Tris buffer, pH 7.5).

  • A tuber lectin from Arisaema helleborifolium Schott with anti-insect activity against melon fruit fly, Bactrocera cucurbitae (Coquillett) and anti-cancer effect on human cancer cell lines

    2006, Archives of Biochemistry and Biophysics
    Citation Excerpt :

    The larvae were then homogenized in the recommended buffer for each enzyme. The activity of esterases was determined by the method of Katzenellenbogen and Kafatos [26] while the activity of acid and alkaline phosphatases were assessed by the method given by Mc Intyre [27]. The results were expressed as means ± SE.

  • Physiology and Biochemistry of Insect Moulting Fluid

    1996, Advances in Insect Physiology
  • Properties of esterases from pharate pupal moulting fluid of the tobacco hornworm, Manduca sexta

    1983, Comparative Biochemistry and Physiology -- Part B: Biochemistry and
View all citing articles on Scopus

Present address: Department of Physiology-Biophysics, University of Illinois, Urbana, Illinois 61801.

View full text