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 vol: 38  issue:3  pages: 44-45
Abstract: 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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Reference: Tsymanovich S.A., Nikandrov V.N., Maksimova R.A., Sharkova T.S., Andreenko G.V., Serebriakova T.N., Physico-chemical properties of the thrombolytic compound longolytin, Voprosy meditsinskoi khimii, 1992, vol: 38(3), 44-45.
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