Biological activity and the 3-methylhistidine content of actin and myosin.

The Biochemical journal ·Vol. 119 ·No. 2 ·1970-09-00 ·Pages 293-8

Johnson P, Perry SV

Abstract

1. The 3-methylhistidine content of myosin varies according to muscle type. It is highest in myosin from white skeletal muscle and lower values are obtained from myosin of red skeletal and smooth muscle. 2. The 3-methylhistidine content of actin was similar in all of the types of muscle from which it was isolated. 3. The 3-methylhistidine of rabbit actin is localized in a single tryptic peptide that was readily modified during fractionation procedures. 4. Photo-oxidation studies indicated that the 3-methylhistidine residues are not essential for adeonsine triphosphatase and actin-combining activities of myosin. 5. During photooxidation G-actin lost completely the ability to polymerize to the F form before all the 3-methylhistidine was destroyed.

MeSH Terms

Adenosine Triphosphatases/analysis Amino Acids/analysis Animals Cattle Columbidae Crustacea Female Histidine/analysis Macromolecular Substances Mice Muscle Proteins/analysis Muscle, Smooth/analysis Muscles/analysis Oxidation-Reduction Peptides/analysis Photochemistry Rabbits Trypsin Uterus

Chemicals

Amino Acids Macromolecular Substances Muscle Proteins Peptides Histidine Trypsin Adenosine Triphosphatases

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Johnson P

Perry S V

References (18)

18 references, click to expand

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Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj1190293

Published

1970-09-00

Pages

293-8

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1179351

Subset

External Links

PubMed source DOI: 10.1042/bj1190293 PMC Full Text View journal details

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Biological activity and the 3-methylhistidine content of actin and myosin.

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