3-methylhistidine in actin and other muscle proteins.
TLDR
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.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.read more
Citations
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Actin and myosin and cell movement.
Thomas D. Pollard,Weihing Rr +1 more
TL;DR: The CRC Critical Reviews in Biochemistry: Vol. 2, No. 1, No. 1, pp. 1-65 as mentioned in this paper, reviewed Actin And Myosin And Cell Movemen.
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Posttranslational covalent modification of proteins
TL;DR: A brief consideration of the questions about where and when the derivatization reactions occur, how the specificity of the reactions is established, and how the posttranslational modifications can facilitate biological processes, reveal a need for more information on all these points.
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An electrophoretic study of the low-molecular-weight components of myosin.
W. T. Perrie,S. V. Perry +1 more
TL;DR: It is suggested that the Differences in the low-molecular-weight components of myosin from different types of muscle are a consequence of differences in the isoenzyme composition of the myosins.
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A new protein of the thick filaments of vertebrate skeletal myofibrils. Extractions, purification and characterization.
TL;DR: The C-protein molecule contains a single polypeptide chain of molecular weight 140,000 and the intrinsic viscosity of 13.6 ml/g suggests that the molecule is neither completely globular nor as elongated as molecules like paramyosin or tropomyosin.
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Carnosine and related substances in animal tissues
TL;DR: Relationships appear to exist between the zoological classification of a species and the identities and relative amounts of its dipeptides, and the reptile skins contained the same di peptides and other substances as their corresponding muscle tissues.
References
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Actin: a comparative study.
Mary E. Carsten,Arnold M. Katz +1 more
TL;DR: Structural differences between actins from species over a wide range of the evolutionary scale are demonstrated; the differences decreased with closer relationship of the specied.
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