Literature DB >> 4268883

Enzymic sulphation of p-nitrophenol and steroids by larval gut tissues of the southern armyworm (Prodenia evidania Cramer).

R S Yang, C F Wilkinson.   

Abstract

1. An enzyme system that catalyses the sulphation of p-nitrophenol, cholesterol, alpha-ecdysone, beta-sitosterol, dehydroepiandrosterone, oestrone and four other steroids of plant and insect origin was obtained from the soluble fraction of southern-armyworm gut tissues. 2. The enzyme system required ATP and inorganic sulphate, and activity was slightly enhanced in the presence of GSH. 3. The properties of this enzyme system with respect to pH, temperature, substrate and protein concentrations and various cofactors and reagents were studied. At -23 degrees C the enzyme preparation could be stored for 2 weeks without drastic loss of activity. At the end of storage for 1 month the loss of activity was approx. 21%. 4. The possible involvement of this enzyme system in insect endocrine control is discussed.

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Year:  1972        PMID: 4268883      PMCID: PMC1174428          DOI: 10.1042/bj1300487

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  22 in total

1.  Kinetic studies on the phenol-sulfate conjugating system of rat liver.

Authors:  H L SEGAL
Journal:  J Biol Chem       Date:  1955-03       Impact factor: 5.157

2.  The enzymatic conjugation of m-aminophenol.

Authors:  S BERNSTEIN; R W MCGILVERY
Journal:  J Biol Chem       Date:  1952-09       Impact factor: 5.157

3.  Kinetic studies of the phenol sulphotranferase reaction.

Authors:  R K Banerjee; A B Roy
Journal:  Biochim Biophys Acta       Date:  1968-03-25

4.  Sterol sulfates in an insect.

Authors:  R F Hutchins; J N Kaplanis
Journal:  Steroids       Date:  1969-05       Impact factor: 2.668

5.  Formation of serotonin O-sulfate by sulfotransferase of rabbit liver.

Authors:  H Hidaka; T Nagatsu; K Yagi
Journal:  Biochim Biophys Acta       Date:  1969-04-01

6.  Microsomal mixed-function oxidases in insects. I. Localization and properties of an enzyme system effecting aldrin epoxidation in larvae of the southern armyworm (Prodenia eridania).

Authors:  R I Krieger; C F Wilkinson
Journal:  Biochem Pharmacol       Date:  1969-06       Impact factor: 5.858

7.  [The ecdysone titer during the development of insects. IV. Development of the lepidopterans Bombyx mori L. and Cerura vinula L].

Authors:  E Shaaya; P Karlson
Journal:  Dev Biol       Date:  1965-06       Impact factor: 3.582

8.  The sulfotransferases of guinea pig liver.

Authors:  R K Banerjee; A B Roy
Journal:  Mol Pharmacol       Date:  1966-01       Impact factor: 4.436

9.  The conjugation of phenols with phosphate in grass grubs and flies.

Authors:  A Binning; F J Darby; M P Heenan; J N Smith
Journal:  Biochem J       Date:  1967-04       Impact factor: 3.857

10.  Purification from rat liver of an enzyme that catalyses the sulphurylation of phenols.

Authors:  F A McEvoy; J Carroll
Journal:  Biochem J       Date:  1971-08       Impact factor: 3.857

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  4 in total

1.  Age-dependent arylsulphatase and sulphotransferase activities in the southern armyworm: a possible insect endocrine regulatory mechanism?

Authors:  R S Yang; J G Pelliccia; C F Wilkinson
Journal:  Biochem J       Date:  1973-11       Impact factor: 3.857

2.  3'-phosphoadenosine-5'-phosphosulphate synthesis and involvement in sulphotransferase reactions in the insect, Spodoptera littoralis.

Authors:  R E Isaac; K K Phua; H H Rees
Journal:  Biochem J       Date:  1982-04-15       Impact factor: 3.857

3.  3-O-hydrosulphato-4-hydroxyphenethylamine (dopamine 3-O-sulphate), a metabolite involved in the sclerotization of insect cuticle.

Authors:  R P Bodnaryk; P C Brunet
Journal:  Biochem J       Date:  1974-03       Impact factor: 3.857

4.  Isolation and identification of apolar metabolites of ingested 20-hydroxyecdysone in frass ofHeliothis virescens larvae.

Authors:  I Kubo; S Komatsu; Y Asaka; G de Boer
Journal:  J Chem Ecol       Date:  1987-04       Impact factor: 2.626

  4 in total

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