Thiolysis of Dinitrophenylated Myosin with Restoration of Adenosine Triphosphatase Activity

Gary Bailin; Michael Bárány

doi:10.1016/s0021-9258(19)44595-x

December 1, 1972Journal of Biological ChemistryOpen Access

Thiolysis of Dinitrophenylated Myosin with Restoration of Adenosine Triphosphatase Activity

View Full Paper

Ask AI

Bookmark

Share

Key Points

To determine whether thiolysis with 2-mercaptoethanol can remove dinitrophenyl groups from chemically modified rabbit skeletal myosin and restore its ATPase activity.
Treated rabbit skeletal myosin containing 1.43 moles of 1-fluoro-2,4-dinitrobenzene per 5 x 10^5 g protein with 0.05 M 2-mercaptoethanol at pH 8.5.
Quantified dinitrophenyl group removal and enzyme reactivation using chemical incorporation measurements and difference spectra.
Treatment with 2-mercaptoethanol cleaved 0.73 moles of the dinitrophenyl group per 5 x 10^5 g protein.
Achieved complete restoration of both K+(EDTA)-ATPase and Ca2+-ATPase enzymatic activities.

No abstract yet

We only have this paper's title and publication details.

Read it at the source

Ask about this paper

Answers are grounded in this paper and cite their sources.

Implication

Biochemical assay reveals 2-mercaptoethanol restores ATPase activity in dinitrophenylated rabbit myosin, indicating reversible chemical inhibition of muscle enzyme function.

Discussion

No takes yet. Share an insight, caveat, or question.

Cite This Study

Bailin et al. (1972) studied this question.

synapsesocial.com/papers/6a81e3863385b84e88b6cdb6 https://doi.org/10.1016/s0021-9258(19)44595-x

View Full Paper

Ask AI

Bookmark

Share

Thiolysis of Dinitrophenylated Myosin with Restoration of Adenosine Triphosphatase Activity

Key Points

No abstract yet

Ask about this paper

Implication

Discussion

Cite This Study

Thiolysis of Dinitrophenylated Myosin with Restoration of Adenosine Triphosphatase Activity

Key Points

No abstract yet

Ask about this paper

Implication

Discussion

Cite This Study

Keep reading

Keep reading