Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 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.

Full text

PDF
122

Images in this article

123Fig. 2.
on p.123

Selected References

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

  1. BARANY M., BIRO N. A., MOLNAR J., STRAUB F. B. Darstellung enzymfreien Aktins durch Umfällung mit Magnesium. Acta Physiol Acad Sci Hung. 1954;5(3-4):369–381. [PubMed] [Google Scholar]
  2. BARGETZI J. P. KUMAR KS, COX DJ, WALSH KA, NEURATH H: THE AMINO ACID COMPOSITION OF BOVINE PANCREATIC CARBOXYPEPTIDASE A. Biochemistry. 1963 Nov-Dec;2:1468–1474. doi: 10.1021/bi00906a046. [DOI] [PubMed] [Google Scholar]
  3. GAETJENS E., THERATTIL ANTONY T., BARANY M. MODIFICATION OF L-MYOSIN BY DISULFIDE-SULFHYDRYL INTERCHANGE REACTION. Biochim Biophys Acta. 1964 Jun 8;86:554–566. doi: 10.1016/0304-4165(64)90095-9. [DOI] [PubMed] [Google Scholar]
  4. HABEEB A. F., CASSIDY H. G., SINGER S. J. Molecular structural effects produced in proteins by reaction with succinic anhydride. Biochim Biophys Acta. 1958 Sep;29(3):587–593. doi: 10.1016/0006-3002(58)90016-7. [DOI] [PubMed] [Google Scholar]
  5. KIELLEY W. W., HARRINGTON W. F. A model for the myosin molecule. Biochim Biophys Acta. 1960 Jul 15;41:401–421. doi: 10.1016/0006-3002(60)90037-8. [DOI] [PubMed] [Google Scholar]
  6. LEADBEATER L., PERRY S. V. The effect of actin on the magnesium-activated adenosine triphosphatase of heavy meromyosin. Biochem J. 1963 May;87:233–239. doi: 10.1042/bj0870233. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. LOWEY S., COHEN C. Studies on the structure of myosin. J Mol Biol. 1962 Apr;4:293–308. doi: 10.1016/s0022-2836(62)80007-2. [DOI] [PubMed] [Google Scholar]
  8. MUELLER H., PERRY S. V. The chromatography of the meromyosins on diethylaminoethylcellulose. Biochem J. 1961 Jul;80:217–223. doi: 10.1042/bj0800217. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. MUELLER H., PERRY S. V. The degradation of heavy meromyosin by trypsin. Biochem J. 1962 Dec;85:431–439. doi: 10.1042/bj0850431. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Mueller H. Characterization of the molecular region containing the active sites of myosin. J Biol Chem. 1965 Oct;240(10):3816–3828. [PubMed] [Google Scholar]
  11. NANKINA V. P., KOFMAN E. B., CHERNIAK V. Ia, KALAMKAROVA M. B. PRODUKTY PROTEOLIZA TIAZHELOGO MEROMIOZINA, OBLADAIUSHCHIE ADENOZINTRIFOSFATAZNO I AKTIVNOST'IU. Biokhimiia. 1964 May-Jun;29:424–431. [PubMed] [Google Scholar]
  12. Nanninga L. B., Mommaerts W. F. STUDIES ON THE FORMATION OF AN ENZYME-SUBSTRATE COMPLEX BETWEEN MYOSIN AND ADENOSINETRIPHOSPHATE. Proc Natl Acad Sci U S A. 1960 Aug;46(8):1155–1166. doi: 10.1073/pnas.46.8.1155. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. PERRY S. V., COTTERILL J. THE ACTION OF THIOL REAGENTS ON THE ADENOSINE-TRIPHOSPHATASE ACTIVITIES OF HEAVY MEROMYOSIN AND L-MYOSIN. Biochem J. 1965 Jul;96:224–230. doi: 10.1042/bj0960224. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. PERRY S. V. The chromatography of L-myosin on diethylaminoethylcellulose. Biochem J. 1960 Jan;74:94–101. doi: 10.1042/bj0740094. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Perry S. V., Cotterill J. Interaction of actin and myosin. Nature. 1965 Apr 10;206(980):161–163. doi: 10.1038/206161a0. [DOI] [PubMed] [Google Scholar]
  16. RICE R. V. Conformation of individual macromolecular particles from myosin solution. Biochim Biophys Acta. 1961 Sep 30;52:602–604. doi: 10.1016/0006-3002(61)90427-9. [DOI] [PubMed] [Google Scholar]
  17. SZENT-GYORGYI A. G. Meromyosins, the subunits of myosin. Arch Biochem Biophys. 1953 Feb;42(2):305–320. doi: 10.1016/0003-9861(53)90360-9. [DOI] [PubMed] [Google Scholar]
  18. WOODS E. F., HIMMELFARB S., HARRINGTON W. F. Studies on the structure of myosin in solution. J Biol Chem. 1963 Jul;238:2374–2385. [PubMed] [Google Scholar]
  19. YOUNG D. M., HIMMELFARB S., HARRINGTON W. F. ON THE STRUCTURAL ASSEMBLY OF THE POLYPEPTIDE CHAINS OF HEAVY MEROMYOSIN. J Biol Chem. 1965 Jun;240:2428–2436. [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES