, Volume 56, Issue 3, pp 153–157 | Cite as

Some properties of the protease from Aspergillus terricola

  • Nadejda A. Zaikina
  • Larisa K. Shataeva
  • N. P. Elinov
  • G. V. Samsonov


The protease from Aspergillus terricola (terrilytin) was isolated and purified by the ion exchange method and by gel chromatography. The data on its molecular weight, isoelectric point, N-terminal amino acids were described. The protease included polysaccharide which stabilized the enzyme activity under the storage and lyophylization. Polysaccharides isolated from different fungi and yeasts were found to stabilize and activate terrilytin rising the affinity of enzyme to substrate. Terrilytin was revealed to exibit the thrombolytic effect and expressive affinity to the fibrin in comparison with other substrates of high and low molecular weight. The enzyme showed the antigenic activity. From immune rabbit sera 7Sγ-globulins inhibiting proteolysis of caseine and 19Sγ-globulins activating the proteolysis of fibrin and fibrinogen by terrilytin were isolated by gel chromatography.


Enzyme Molecular Weight Chromatography Enzyme Activity Polysaccharide 
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Copyright information

© Dr. W. Junk bv - Publishers 1975

Authors and Affiliations

  • Nadejda A. Zaikina
    • 1
  • Larisa K. Shataeva
    • 1
  • N. P. Elinov
    • 1
  • G. V. Samsonov
    • 1
  1. 1.Chemical Pharmaceutical InstituteLeningradUSSR

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