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. 1966 Jul;100(1):120–130. doi: 10.1042/bj1000120

The biological activity of subfragment 1 prepared from heavy meromyosin

J M Jones 1, S V Perry 1
PMCID: PMC1265102  PMID: 4225874

Abstract

1. The action of trypsin, chymotrypsin and subtilisin on the adenosine-triphosphatase and actin-combining activities, as measured by viscometric means, of H-meromyosin were compared. 2. Subfragment 1 produced by prolonged tryptic digestion has a molecular weight of 129000. 3. The preparations isolated by gel filtration and actin combination were shown to be similar. 4. Subfragment-1 preparations possess appreciably higher adenosine-triphosphatase activities than H-meromyosin when related to total nitrogen. 5. Chromatographic and gelfiltration studies indicated that adenosine-triphosphatase activity is not distributed uniformly in all fractions of subfragment 1. 6. The Ca2+-activated adenosine triphosphatase of subfragment 1 was stimulated by thiol reagents in a similar fashion to myosin and H-meromyosin. 7. Subfragment 1 differed from myosin and H-meromyosin in that its adenosine triphosphatase was only slightly activated by Mg2+ in the presence of actin. 8. A subfragment-1-like component was obtained by chymotryptic digestion of H-meromyosin. 9. The results obtained from enzymic and hydrodynamic studies and from amino acid analyses are compatible with the concept of one molecule of H-meromyosin giving rise to one molecule of subfragment 1 on proteolytic digestion.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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