Electrophoretic purification of soluble trehalase from Drosophila melanogaster by selective unstacking

T. A. Bargiello; J. Grossfield

doi:10.1016/0003-2697(80)90051-2

Electrophoretic purification of soluble trehalase from Drosophila melanogaster by selective unstacking

T. A. Bargiello, J. Grossfield

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

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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 K_m 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 language	English (US)
Pages (from-to)	131-137
Number of pages	7
Journal	Analytical Biochemistry
Volume	101
Issue number	1
DOIs	https://doi.org/10.1016/0003-2697(80)90051-2
State	Published - Jan 1 1980
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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title = "Electrophoretic purification of soluble trehalase from Drosophila melanogaster by selective unstacking",

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.",

author = "Bargiello, {T. A.} and J. Grossfield",

note = "Funding Information: This work was supported in part by National Institutes of Health Grant GM 21360 and CUNY FRAP 10576. We also wish to thank an anonymous reviewer for detailed comments and suggestions on previous draft of this manuscript.",

year = "1980",

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doi = "10.1016/0003-2697(80)90051-2",

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T1 - Electrophoretic purification of soluble trehalase from Drosophila melanogaster by selective unstacking

AU - Bargiello, T. A.

AU - Grossfield, J.

N1 - Funding Information: This work was supported in part by National Institutes of Health Grant GM 21360 and CUNY FRAP 10576. We also wish to thank an anonymous reviewer for detailed comments and suggestions on previous draft of this manuscript.

PY - 1980/1/1

Y1 - 1980/1/1

N2 - 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.

AB - 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.

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Electrophoretic purification of soluble trehalase from Drosophila melanogaster by selective unstacking

Abstract

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