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
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Publikationsdatum:
21. Juni 2018 (online)

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;
  • 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;
  • 3 Kline D. L. The purification and crystallization of plasminogen (profibrinolysin). J. biol. Chem. 204: 949 1953;
  • 4 Remmert L. F, Cohen P. P. Partial purification and properties of a proteolytic enzyme of human serum. J. biol. Chem. 181: 431 1949;
  • 5 Shulman S. Purification and identification of components of human plasminogen. Biochim. biophys. Acta. 46: 6 1961;
  • 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;
  • 7 Biserte G, Osteux R. La chromatographie de partage sur papier des dinitro-phenyl amino acides. Bull. Soc. chim. biol. 33: 50 1951;
  • 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;
  • 9 McFadden M. L, Smith E. L. Free amino groups and N-terminal sequence of rabbit antibodies. J. biol. Chem. 214: 185 1955;
  • 10 Davies M. C, Englert M. E. Physical properties of highly purified human plasminogen. J. biol. Chem. 235: 1011 1960;
  • 11 Rifé U, Shulman S. Molecular changes in activation of plasminogen. Fed. Proc. 19: 59 1960;
  • 12 Shulman S, Rife U. Some aspects of the plasminogen activation mechanism. Thromb Diath. haem. in press..