Purification and properties of a fibrinolytic enzyme fromBacillus subtilis
- 1 January 1980
- journal article
- Published by Wiley in Journal of Basic Microbiology
- Vol. 20 (6) , 375-382
- https://doi.org/10.1002/jobm.3630200603
Abstract
A fibrinolytic enzyme obtained from B. subtilis was purified, using DEAE-cellulose column chromatography, and gel filtration on Sephadex G-100. The preparation was homogeneous as tested by gel filtration on Sephadex G-200, and disc electrophoresis. The molecular weight of this enzyme was 29.400 estimated by gel filtration on Sephadex G-100. The optimum pH for enzyme activity was 7.2 Copper ions significantly increased enzyme activity, while Zn++ and Mn++ caused marked inhibition.Keywords
This publication has 10 references indexed in Scilit:
- Partial Purification and Some Enzymatic Properties of a Proteinase from Aeromonas proteolyticaExperimental Biology and Medicine, 1969
- Purification and some properties of a protease from Alternaria tenuissimaArchives of Biochemistry and Biophysics, 1969
- Some properties of the extracellular proteolytic enzymes of the milk-spoiling organismPseudomonas aeruginosaATCC 10145Journal of Dairy Research, 1968
- SIMPLIFIED “DISC” (POLYACRYLAMIDE GEL) ELECTROPHORESIS*Annals of the New York Academy of Sciences, 1964
- Estimation of the molecular weights of proteins by Sephadex gel-filtrationBiochemical Journal, 1964
- B. Subtilis neutral protease, a zinc enzyme of high activityBiochemical and Biophysical Research Communications, 1964
- [1] Column chromatography of proteins: Substituted cellulosesPublished by Elsevier ,1962
- [5] Plant proteolytic enzymesPublished by Elsevier ,1955
- The Determination of Enzyme Dissociation ConstantsJournal of the American Chemical Society, 1934