June 1, 1985Journal of Biological ChemistryOpen Access

Actin-binding peptide obtained by the cyanogen bromide cleavage of the 20-kDa fragment of myosin subfragment-1.

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Population

20-kDa fragment of myosin subfragment-1 heavy chain (in vitro biochemical model)

Design

Preclinical

Authors

TKT. KatohGifu University HKHironori KatohKyushu University FMFumi MoritaHokkaido University of Science

Discussion

Member takes

Implication

May guide sarcomere research in heart failure models; leaves open in vivo roles of SH1/SH2 sites.

Structured PICO

Population

20-kDa fragment of myosin subfragment-1 heavy chain (in vitro biochemical model)

Intervention

Cyanogen bromide cleavage and renaturation procedure

Outcome

Affinity of the 10-kDa peptide for F-actin (apparent dissociation constant)surrogate

The study identifies a 10-kDa peptide from myosin subfragment-1 that binds to F-actin with an apparent dissociation constant of 0.94 microM, supporting the existence of an actin-binding site around the SH1 and SH2 groups.

Cite This Study

Katoh et al. (1985) studied this question.

synapsesocial.com/papers/6a714320c92390ac2d07ec9b https://doi.org/10.1016/s0021-9258(18)88839-1

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Actin-binding peptide obtained by the cyanogen bromide cleavage of the 20-kDa fragment of myosin subfragment-1.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Actin-binding peptide obtained by the cyanogen bromide cleavage of the 20-kDa fragment of myosin subfragment-1.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider