Electrophoretic purification of soluble trehalase from Drosophila melanogaster by selective unstacking

T. A. Bargiello, J. Grossfield

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Specific activity of soluble trehalase from Drosophila melanogaster has been increased at least 10 times by preparative electrophoresis using selective unstacking. However, enzyme yield was poor, with only 17% of the original activity recovered. A comparison of Km of crude and partially purified trehalase revealed no difference (0.650 and 0.666 mm, respectively). Electrophoretic parameters for a modified version of multiphasic buffer system 4014 are described and electrophoretic parameters which may be utilized in the electrophoretic purification of trehalase from 17 species of Drosophila are reported.

Original languageEnglish (US)
Pages (from-to)131-137
Number of pages7
JournalAnalytical Biochemistry
Volume101
Issue number1
DOIs
StatePublished - Jan 1 1980
Externally publishedYes

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Trehalase
Drosophila melanogaster
Purification
Electrophoresis
Drosophila
Buffers
Enzymes

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Electrophoretic purification of soluble trehalase from Drosophila melanogaster by selective unstacking. / Bargiello, T. A.; Grossfield, J.

In: Analytical Biochemistry, Vol. 101, No. 1, 01.01.1980, p. 131-137.

Research output: Contribution to journalArticle

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