Purification of Ca-7, a Thrombolytic Fungal Protease

Ives, D. A. J.; Tosoni, Anthony L.

doi:10.1139/o67-122

Cited by 10 publications

(3 citation statements)

References 11 publications

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“…In several of its properties S. brevicaulis protease resembles Protease I (3-7), CA-7 (15), and other alkaline proteases. It has an average molecular weight of 24 000 compared to 22 000 (also 32 000) reported for CA-7 (1 5).…”

Section: Discussionmentioning

confidence: 99%

“…Bergkvist (3: 4, 5, 6, 7) p~~blished a series of papers dealing with isolation and properties of Protease I, an enzyme isolated from A. oryzae. Jves and Tosoni (15) p~irified Aspergillin 0 to obtain a highly active preparation called CA-7, probably identical with protease I of Bergkvist. This enzyme has been st~tdied extensively as a thrombolytic agent in animals by Roschlau and coworkers (22,23,24).…”

Section: Introductionmentioning

confidence: 99%

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An extracellular proteolytic enzyme from Scopulariopsis brevicaulis. 1. Purification and properties

Singh¹,

Vézina²

1971

Can. J. Microbiol.

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A proteolytic enzyme present in culture filtrates of Scopulariopsis brevicaulis was purified about 200-fold by (NH4)2SO4 and ethanol fractionations followed by chromatography on DEAE-cellulose, DEAE-Sephadex, and hydroxylapatite. Ultracentrifugation of the purified enzymes showed only one sedimenting component and its molecular weight was estimated to be about 24 000. The protease hydrolyzed casein, urea-denatured hemoglobin, gelatin, fibrinogen, fibrin, insulin chains A and B, but not human serum albumin or ovalbumin. It also coagulated milk. The enzyme had no action on the various peptides tested and showed low esterase activity. Optimum pH for casein hydrolysis was 10.5 to 11; for hemoglobin hydrolysis 7.0–9.5, and for gelatin hydrolysis, 6.0–8.0. The enzyme activity was unaffected by most metal ions, SH-reagents, and some natural trypsin inhibitors. The protease was strongly inhibited by diisopropylfluorophosphate and phenylmethanesulfonyl fluoride. Although similar in some respects to CA-7, the enzyme isolated from Aspergillus oryzae, and other alkaline proteases, the S. brevicaulis protease does not appear to be identical with any one of them.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

An extracellular proteolytic enzyme from Scopulariopsis brevicaulis. 1. Purification and properties

Singh¹,

Vézina²

1971

Can. J. Microbiol.

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“…Preparation and purification of the enzyme has taken place according to methods described by Ives and Tosoni (1967). The enzyme was used as a freeze-dried, sterile and pyrogen-free preparation in 50 ml vials containing 50,000 Ca-units (lots 1009, 1011).…”

Section: Proteolytic Enzymementioning

confidence: 99%

Proteolytic Inhibitors in Plasma from Man Treated with a Protease from Aspergillus oryzae

Jurgens

Lindvall

Magnuson

et al. 1970

Acta Physiologica Scandinavica

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The level of total, heat stable and heat labile inhibitors of a proteolytic enzyme from Aspergillus oryzae‐protease I‐have been studied in plasma from eight patients. After treatment of these patients by infusions of 150 mg of the proteolytic enzyme in 5 % levulose solution, the change in the level of the different inhibitors have been estimated. It has been shown that there is a lowering of the total inhibitors content after each infusion. This decrease is only partly compensated for by the day following the first infusion. After the forthcoming infusions the decrease is completely compensated for resulting in a level before each subsequent infusion which is lower than that before commencement of treatment. This remaning decrease can be attributed to the heat stable inhibitor. A possible mechanism for the thrombolytic effect of the protease is mentioned.

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Purification and some properties of pure Cochliobolus lunatus fibrinolytic Enzyme

Abdelfattah¹,

Ismail²

1984

Biotech & Bioengineering

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Purification of partially purified fibrinolytic enzyme was attempted by chromatography on DEAE-cellulose (D-52) column. The results indicated the resolution of three protein components and one minor component. It was shown that the first component was the major of the applied sample. Examination of fibrinolytic activity of the different fractions of components one and two indicated that only the first component possessed fibrinolytic activity. Fibrinolytic activity of the applied sample was completely recovered by the first enzyme component, and the most active fraction of this enzyme component showed 3.3-fold purification. The pure fibrinolytic enzyme was relatively more stable at pH 6.98, which was also optimal for its activity. After heating the enzyme solution (pH = 6.98) at 55 and 60 degrees C for 15 min, the enzyme still retained 34.7 and 17.3% of its original activity, respectively. Zinc ions partially inhibited the enzyme. Copper ions activated the enzyme. Iodine partially inhibited the fungal fibrinolytic enzyme at a final concentration of 10(-4)M; at 10(-2)M complete inactivation was brought about. The p-chloromercuribenzoate at a final concentration of 10(-2)M brought about partial inhibition whereby the enzyme lost about 33% of its original activity. Reduced glutathione brought about activation of the enzyme, while trypsin inhibitor did not show any effect on enzyme activity.

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Purification of Ca-7, a Thrombolytic Fungal Protease

Cited by 10 publications

References 11 publications

An extracellular proteolytic enzyme from Scopulariopsis brevicaulis. 1. Purification and properties

An extracellular proteolytic enzyme from Scopulariopsis brevicaulis. 1. Purification and properties

Proteolytic Inhibitors in Plasma from Man Treated with a Protease from Aspergillus oryzae

Purification and some properties of pure Cochliobolus lunatus fibrinolytic Enzyme

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