Graphical evaluation of alkylation of myosin's SH1 and SH2: The N- phenylmaleimide reaction

Ling Xie; Wan Xia Li; Vincent A Barnett; Mark Schoenberg

doi:10.1016/S0006-3495(97)78720-4

Graphical evaluation of alkylation of myosin's SH1 and SH2: The N- phenylmaleimide reaction

Ling Xie, Wan Xia Li, Vincent A Barnett, Mark Schoenberg

Integrative Biology and Physiology

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Abstract

Previous assertions about the effect of alkylation of SIll and SH2 on the myosin high-salt calcium and EDTA ATPases have been summarized, and a simple procedure for obtaining the fractional labeling of SIll and SH2 after treatment of myosin with alkylating agents has been derived. A simple graphical procedure for illustrating the degree of preference of a particular alkylating agent for SIll over SH2 has also been developed. The procedures we developed were validated by applying them to two previously studied compounds, 4-(2-iodoacetamido)-TEMPO and 2,4-dinitrofluorobenzine, and then were used to determine a procedure for maximizing the extent of labeling of SIll alone by N-phenylmaleimide, a compound not previously studied in this manner. It was found that ~80% of the SIll sites could be alkylated without significant alkylation of SH2.

Original language	English (US)
Pages (from-to)	858-865
Number of pages	8
Journal	Biophysical journal
Volume	72
Issue number	2 I
DOIs	https://doi.org/10.1016/S0006-3495(97)78720-4
State	Published - Feb 1997

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title = "Graphical evaluation of alkylation of myosin's SH1 and SH2: The N- phenylmaleimide reaction",

abstract = "Previous assertions about the effect of alkylation of SIll and SH2 on the myosin high-salt calcium and EDTA ATPases have been summarized, and a simple procedure for obtaining the fractional labeling of SIll and SH2 after treatment of myosin with alkylating agents has been derived. A simple graphical procedure for illustrating the degree of preference of a particular alkylating agent for SIll over SH2 has also been developed. The procedures we developed were validated by applying them to two previously studied compounds, 4-(2-iodoacetamido)-TEMPO and 2,4-dinitrofluorobenzine, and then were used to determine a procedure for maximizing the extent of labeling of SIll alone by N-phenylmaleimide, a compound not previously studied in this manner. It was found that ~80% of the SIll sites could be alkylated without significant alkylation of SH2.",

author = "Ling Xie and Li, {Wan Xia} and Barnett, {Vincent A} and Mark Schoenberg",

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T1 - Graphical evaluation of alkylation of myosin's SH1 and SH2

T2 - The N- phenylmaleimide reaction

AU - Xie, Ling

AU - Li, Wan Xia

AU - Barnett, Vincent A

AU - Schoenberg, Mark

PY - 1997/2

Y1 - 1997/2

N2 - Previous assertions about the effect of alkylation of SIll and SH2 on the myosin high-salt calcium and EDTA ATPases have been summarized, and a simple procedure for obtaining the fractional labeling of SIll and SH2 after treatment of myosin with alkylating agents has been derived. A simple graphical procedure for illustrating the degree of preference of a particular alkylating agent for SIll over SH2 has also been developed. The procedures we developed were validated by applying them to two previously studied compounds, 4-(2-iodoacetamido)-TEMPO and 2,4-dinitrofluorobenzine, and then were used to determine a procedure for maximizing the extent of labeling of SIll alone by N-phenylmaleimide, a compound not previously studied in this manner. It was found that ~80% of the SIll sites could be alkylated without significant alkylation of SH2.

AB - Previous assertions about the effect of alkylation of SIll and SH2 on the myosin high-salt calcium and EDTA ATPases have been summarized, and a simple procedure for obtaining the fractional labeling of SIll and SH2 after treatment of myosin with alkylating agents has been derived. A simple graphical procedure for illustrating the degree of preference of a particular alkylating agent for SIll over SH2 has also been developed. The procedures we developed were validated by applying them to two previously studied compounds, 4-(2-iodoacetamido)-TEMPO and 2,4-dinitrofluorobenzine, and then were used to determine a procedure for maximizing the extent of labeling of SIll alone by N-phenylmaleimide, a compound not previously studied in this manner. It was found that ~80% of the SIll sites could be alkylated without significant alkylation of SH2.

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Graphical evaluation of alkylation of myosin's SH1 and SH2: The N- phenylmaleimide reaction

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