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August 1, 1975Journal of Biological ChemistryOpen Access

The primary structure of actin from rabbit skeletal muscle. Five cyanogen bromide peptides, including the NH2 and COOH termini.

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Key result

The sequences of five cyanogen bromide peptides of actin from rabbit skeletal muscle were determined, revealing that Cys-373 is the first to react with N-ethylmaleimide.

Population

Rabbit skeletal muscle actin

Design

Preclinical

Authors

MEMarshall ElzingaHeart Failure / CardiomyopathyJCJohn H. CollinsDuke University

Discussion

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Implication

No immediate clinical implications in cardiology; leaves open Cys-373 relevance to human cardiac actin function.

Structured PICO

P
Population
Rabbit skeletal muscle actin
I
Intervention
Cyanogen bromide cleavage and amino acid sequencing
O
Outcome
Amino acid sequences of five cyanogen bromide peptides

This study determined the amino acid sequence of five cyanogen bromide peptides of rabbit skeletal muscle actin, including the NH2 and COOH termini.

Cite This Study

Elzinga et al. (1975) studied this question. The sequences of five cyanogen bromide peptides of actin from rabbit skeletal muscle were determined, revealing that Cys-373 is the first to react with N-ethylmaleimide.

synapsesocial.com/papers/6a0cdadaedb32e8d900261eehttps://doi.org/10.1016/s0021-9258(19)41137-x
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Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1The primary structure of actin from rabbit skeletal muscle. Three cyanogen bromide peptides that are insoluble at neutral pH.1975 · 15 citations
  2. 2Amino acid sequence around the single 3-methylhistidine residue in rabbit skeletal muscle myosin1971 · 77 citations
  3. 3N-Terminal Sequence of Actin*1966 · 32 citations
  4. 4Modification of an Arginyl Residue in Pepsin by 2,3-Butanedione1972 · 43 citations