Download PDF
Thromb Haemost 1961; 05(03): 396-401
DOI: 10.1055/s-0038-1654934
Originalarbeiten – Original Article – Travaux Originaux
Schattauer GmbH

Preliminary Studies on the N-Terminal Amino Acids of Human Plasminogen[*]

Sidney Shulman   **
1   Department of Biophysics, University of Buffalo School of Medicine, Buffalo, N.Y., USA
,
Ubaldo Rifé
1   Department of Biophysics, University of Buffalo School of Medicine, Buffalo, N.Y., USA
› Author Affiliations
Further Information

Publication History

Publication Date:
21 June 2018 (online)

Also available at
    Permissions and Reprints

Summary

Human plasminogen has been analyzed for N-terminal amino acids. It was found to have one residue each of lysine and serine per molecule, with the possibility that threonine and glutamic acid may also serve in this role. On conversion to SK-plasmin, serine is lost as a terminal group and leucine appears as a new terminal unit.

* This investigation was supported in part by a research grant, H-l792, from the National Heart Institute, Public Health Service, and a research grant from the Heart Association of Erie County.


** Supported by a Senior Research Fellowship (SF-118) from the Public Health Service.


 

  • References

  • 1 Shulman S, Alkjaersig N, Sherry S. Physicochemical studies on human plasminogen (profibrinolysin) and plasmin (fibrinolysin). J. biol. Chem. 233: 91 1958;
    PubMedSearch in Google Scholar
  • 2 Sgouris J. T, Inman J. K, McCall K. B. Starchgel and moving boundary electrophoresis of highly purified profibrinolysin. Biochem. Biophys. Res. Communs. 02: 40 1960;
    CrossrefPubMedSearch in Google Scholar
  • 3 Kline D. L. The purification and crystallization of plasminogen (profibrinolysin). J. biol. Chem. 204: 949 1953;
    PubMedSearch in Google Scholar
  • 4 Remmert L. F, Cohen P. P. Partial purification and properties of a proteolytic enzyme of human serum. J. biol. Chem. 181: 431 1949;
    PubMedSearch in Google Scholar
  • 5 Shulman S. Purification and identification of components of human plasminogen. Biochim. biophys. Acta. 46: 6 1961;
    CrossrefPubMedSearch in Google Scholar
  • 6 Fraenkel-Conrat Harris J. I, Levy A. L. Recent developments in techniques for terminal and sequence studies in peptides and proteins. Methods of Biochemical Analysis 02: 359 1955;
    PubMedSearch in Google Scholar
  • 7 Biserte G, Osteux R. La chromatographie de partage sur papier des dinitro-phenyl amino acides. Bull. Soc. chim. biol. 33: 50 1951;
    PubMedSearch in Google Scholar
  • 8 Levy A. L, Geschwind I. I, Li C. H. Corticotropins (ACTH). II. amino acid composition of a-corticotropin. J. biol. Chem. 213: 187 1953;
    PubMedSearch in Google Scholar
  • 9 McFadden M. L, Smith E. L. Free amino groups and N-terminal sequence of rabbit antibodies. J. biol. Chem. 214: 185 1955;
    PubMedSearch in Google Scholar
  • 10 Davies M. C, Englert M. E. Physical properties of highly purified human plasminogen. J. biol. Chem. 235: 1011 1960;
    PubMedSearch in Google Scholar
  • 11 Rifé U, Shulman S. Molecular changes in activation of plasminogen. Fed. Proc. 19: 59 1960;
    PubMedSearch in Google Scholar
  • 12 Shulman S, Rife U. Some aspects of the plasminogen activation mechanism. Thromb Diath. haem. in press..
    PubMed