Effects of substrate and substrate analogues on the trinitrophenylation of myosin

A. Mühlrad; F. Fábián

doi:10.1016/0005-2728(70)90234-3

Effects of substrate and substrate analogues on the trinitrophenylation of myosin

A. Mühlrad^*, F. Fábián

^*Corresponding author for this work

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

15 Scopus citations

Abstract

The effects of ATP, ATP analogues, Mg²⁺ and actin on the trinitrophenylation of myosin and on the enzymic properties of trinitrophenylated samples were studied. 1. 1. Trinitrophenylation of myosin was inhibited by the presence of ATP and its analogues during the treatment in the order ADP > ATP > pyrophosphate > AMP. 2. 2. The alteration of the enzymic properties due to trinitrophenylation of myosin was prevented by the presence of ATP or ADP and somewhat less by that of pyrophosphate and AMP during trinitrophenylation, but only if Mg²⁺ was also present. 3. 3. Neither the degree of trinitrophenylation nor the enzymic properties of the trinitrophenylated myosin were influenced by the presence of actin during the treatment of myosin.

Original language	English
Pages (from-to)	422-427
Number of pages	6
Journal	Biochimica et Biophysica Acta - Bioenergetics
Volume	216
Issue number	2
DOIs	https://doi.org/10.1016/0005-2728(70)90234-3
State	Published - 1 Sep 1970
Externally published	Yes

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abstract = "The effects of ATP, ATP analogues, Mg2+ and actin on the trinitrophenylation of myosin and on the enzymic properties of trinitrophenylated samples were studied. 1. 1. Trinitrophenylation of myosin was inhibited by the presence of ATP and its analogues during the treatment in the order ADP > ATP > pyrophosphate > AMP. 2. 2. The alteration of the enzymic properties due to trinitrophenylation of myosin was prevented by the presence of ATP or ADP and somewhat less by that of pyrophosphate and AMP during trinitrophenylation, but only if Mg2+ was also present. 3. 3. Neither the degree of trinitrophenylation nor the enzymic properties of the trinitrophenylated myosin were influenced by the presence of actin during the treatment of myosin.",

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AU - Fábián, F.

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N2 - The effects of ATP, ATP analogues, Mg2+ and actin on the trinitrophenylation of myosin and on the enzymic properties of trinitrophenylated samples were studied. 1. 1. Trinitrophenylation of myosin was inhibited by the presence of ATP and its analogues during the treatment in the order ADP > ATP > pyrophosphate > AMP. 2. 2. The alteration of the enzymic properties due to trinitrophenylation of myosin was prevented by the presence of ATP or ADP and somewhat less by that of pyrophosphate and AMP during trinitrophenylation, but only if Mg2+ was also present. 3. 3. Neither the degree of trinitrophenylation nor the enzymic properties of the trinitrophenylated myosin were influenced by the presence of actin during the treatment of myosin.

AB - The effects of ATP, ATP analogues, Mg2+ and actin on the trinitrophenylation of myosin and on the enzymic properties of trinitrophenylated samples were studied. 1. 1. Trinitrophenylation of myosin was inhibited by the presence of ATP and its analogues during the treatment in the order ADP > ATP > pyrophosphate > AMP. 2. 2. The alteration of the enzymic properties due to trinitrophenylation of myosin was prevented by the presence of ATP or ADP and somewhat less by that of pyrophosphate and AMP during trinitrophenylation, but only if Mg2+ was also present. 3. 3. Neither the degree of trinitrophenylation nor the enzymic properties of the trinitrophenylated myosin were influenced by the presence of actin during the treatment of myosin.

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Effects of substrate and substrate analogues on the trinitrophenylation of myosin

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