VOPROSY MEDITSINSKOI KHIMII (ISSN 0042-8809)

Physico-chemical properties of the thrombolytic compound longolytin

   
Tsymanovich S.A., Nikandrov V.N., Maksimova R.A., Sharkova T.S., Andreenko G.V., Serebriakova T.N.
PubMed Id: 1413650
Year: 1992  Volume: 38  Issue: 3  Pages: 44-45
A preparation exhibiting high fibrinolytic activity and ability to activate plasminogen was isolated from cultivation medium of Arthrobotrys longa. Homogeneous protein, obtained after gel filtration on Sephadex G-100, had molecular mass 28,600, pI-3.68-3.74, optimum activity at pH 6.0-9.0 and temperature optimum at 37 degrees. The enzyme proved to be serine proteinase as shown by analysis using inhibitors; it required thiol groups.
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Tsymanovich, S. A., Nikandrov, V. N., Maksimova, R. A., Sharkova, T. S., Andreenko, G. V., Serebriakova, T. N. (1992). Physico-chemical properties of the thrombolytic compound longolytin. Voprosy Meditsinskoi Khimii, 38(3), 44-45.
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