Phosvitin phosphate content. Implications for protein kinase assay

Khalil Ahmed; Michael J. Wilson; Alan T. Davis

doi:10.1016/0005-2744(75)90288-0

Phosvitin phosphate content. Implications for protein kinase assay

Khalil Ahmed, Michael J. Wilson, Alan T. Davis

Laboratory Medicine and Pathology

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

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Abstract

The maximal rates of the protein kinase (ATP: protein phosphotransferase, EC 2.7.1.37) reaction studied with chicken egg yolk phosvitin as substrate are dependent on the level of dephosphorylation of phosvitin. 30% dephospho-phosvitin gives the optimal initial rates. With varying levels of dephosphorylation, the apparent K_m for the substrate also changes in a biphasic manner. If this factor is taken into account, and a suitable adjustment is made for the concentration of dephospho-phosvitin in the reaction, it is possible to achieve maximal rates for the kinase reaction with phosvitin preparations of varying levels of dephosphorylation. Such a consideration is important for comparing the results of protein kinase studies using phosvitin as the substrate.

Original language	English (US)
Pages (from-to)	80-83
Number of pages	4
Journal	BBA - Enzymology
Volume	377
Issue number	1
DOIs	https://doi.org/10.1016/0005-2744(75)90288-0
State	Published - Jan 23 1975

Bibliographical note

Funding Information:
This work is supported in part by research grant No. CA-15062 from N.C.I., N.I.H., U.S.P.H.S.

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10.1016/0005-2744(75)90288-0

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title = "Phosvitin phosphate content. Implications for protein kinase assay",

abstract = "The maximal rates of the protein kinase (ATP: protein phosphotransferase, EC 2.7.1.37) reaction studied with chicken egg yolk phosvitin as substrate are dependent on the level of dephosphorylation of phosvitin. 30\% dephospho-phosvitin gives the optimal initial rates. With varying levels of dephosphorylation, the apparent Km for the substrate also changes in a biphasic manner. If this factor is taken into account, and a suitable adjustment is made for the concentration of dephospho-phosvitin in the reaction, it is possible to achieve maximal rates for the kinase reaction with phosvitin preparations of varying levels of dephosphorylation. Such a consideration is important for comparing the results of protein kinase studies using phosvitin as the substrate.",

author = "Khalil Ahmed and Wilson, \{Michael J.\} and Davis, \{Alan T.\}",

note = "Funding Information: This work is supported in part by research grant No. CA-15062 from N.C.I., N.I.H., U.S.P.H.S.",

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AU - Ahmed, Khalil

AU - Wilson, Michael J.

AU - Davis, Alan T.

N1 - Funding Information: This work is supported in part by research grant No. CA-15062 from N.C.I., N.I.H., U.S.P.H.S.

PY - 1975/1/23

Y1 - 1975/1/23

N2 - The maximal rates of the protein kinase (ATP: protein phosphotransferase, EC 2.7.1.37) reaction studied with chicken egg yolk phosvitin as substrate are dependent on the level of dephosphorylation of phosvitin. 30% dephospho-phosvitin gives the optimal initial rates. With varying levels of dephosphorylation, the apparent Km for the substrate also changes in a biphasic manner. If this factor is taken into account, and a suitable adjustment is made for the concentration of dephospho-phosvitin in the reaction, it is possible to achieve maximal rates for the kinase reaction with phosvitin preparations of varying levels of dephosphorylation. Such a consideration is important for comparing the results of protein kinase studies using phosvitin as the substrate.

AB - The maximal rates of the protein kinase (ATP: protein phosphotransferase, EC 2.7.1.37) reaction studied with chicken egg yolk phosvitin as substrate are dependent on the level of dephosphorylation of phosvitin. 30% dephospho-phosvitin gives the optimal initial rates. With varying levels of dephosphorylation, the apparent Km for the substrate also changes in a biphasic manner. If this factor is taken into account, and a suitable adjustment is made for the concentration of dephospho-phosvitin in the reaction, it is possible to achieve maximal rates for the kinase reaction with phosvitin preparations of varying levels of dephosphorylation. Such a consideration is important for comparing the results of protein kinase studies using phosvitin as the substrate.

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Phosvitin phosphate content. Implications for protein kinase assay

Abstract

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