@article{bdf2c9371aba45f8a3ae485729c6c1a4,
title = "Preparation of homogeneous juvenile hormone specific esterase from the haemolymph of the tobacco hornworm, Manduca sexta",
abstract = "Juvenile hormone specific esterase has been purified to homogeneity from the haemolymph of Manduca sexta by a combination of gel permeation, ion exchange and hydroxylapatite chromatography. The pure esterase has a molecular weight of 68,000 and consists of a single peptide chain. Juvenile hormone specific esterase hydrolyzes JH I at about twice the rate as JH III, has appreciable activity against methyl farnesenate, but does not hydrolyze 1-naphthyl acetate. The homogeneous enzyme is stable for several months when stored at low temperature.",
keywords = "Juvenile hormone, Manduca sexta, esterase, haemolymph",
author = "Coudron, {Thomas A.} and Dunn, {Peter E.} and Seballos, {Hidelisa L.} and Wharen, {Robert E.} and Sanburg, {Larry L.} and Law, {John H.}",
note = "Funding Information: Acknowledgements--This work was supported by grants from the National Science Foundation, No. PCM 7421379, National Institute of General Medical Sciences, No. GM 13863, and from the National Institute of Arthritis, Metabolic and Digestive Diseases, No. AM 05929. Copyright: Copyright 2014 Elsevier B.V., All rights reserved.",
year = "1981",
doi = "10.1016/0020-1790(81)90080-9",
language = "English (US)",
volume = "11",
pages = "453--461",
journal = "Insect Biochemistry and Molecular Biology",
issn = "0965-1748",
publisher = "Elsevier Limited",
number = "4",
}