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- P. Johnson
- Department of Biochemistry, University of Birmingham
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- C I Harris
- Department of Biochemistry, University of Birmingham
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- S V Perry
- Department of Biochemistry, University of Birmingham
書誌事項
- 公開日
- 1967-10-01
- DOI
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- 10.1042/bj1050361
- 公開者
- Portland Press Ltd.
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説明
<jats:p>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.</jats:p>
収録刊行物
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- Biochemical Journal
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Biochemical Journal 105 (1), 361-370, 1967-10-01
Portland Press Ltd.