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Cited by 246

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

3-Methylhistidine in actin and other muscle proteins

Open access
Johnson, P., Harris, C I, Perry, S V·1967·Biochemical Journal

Abstract

1. By the use of the extended elution system for basic amino acid analysis, 3-methylhistidine has been detected in hydrolysates of actin isolated from mammalian, fish and bird skeletal muscle. 2. Evidence is presented to indicate that 3-methylhistidine forms part of the primary structure and that in rabbit actin this residue is restricted to one peptide fraction obtained from the tryptic digest. 3. Rabbit skeletal-muscle actin has a 3-methylhistidine:histidine ratio 1:7·6, indicating a minimum molecular weight of 47600. 4. Adult rabbit myosin contains approximately 2 3-methylhistidine residues/mol. These residues are localized in the heavy meromyosin part of the molecule, and are restricted to the major component obtained after succinylation.

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Crossref · 10.1042/bj1050361

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Metadata

Authors
Johnson, P., Harris, C. I., & Perry, S. V.
Venue
Biochemical Journal
Published
1967-10-01
Volume
105
Issue
1
Pages
361-370
ISSN
0306-3283 (ISSN-L)
OpenAlex
W303113995
Cited by
246
References
1
FWCI
9.20
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: 3-Methylhistidine in actin and other muscle proteins. https://app.cochat.ai/papers/10.1042/bj1050361
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Johnson, P., Harris, C. I., & Perry, S. V. (1967). 3-Methylhistidine in actin and other muscle proteins. Biochemical Journal. https://doi.org/10.1042/bj1050361

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.