scholarly journals An Alkaline Serine-Proteinase from a Bacterium Isolated from Bat Feces: Purification and Characterization

2009 ◽  
Vol 73 (11) ◽  
pp. 2393-2398 ◽  
Author(s):  
Somporn TANSKUL ◽  
Kazumi HIRAGA ◽  
Katsumi TAKADA ◽  
Suchart RUNGRATCHOTE ◽  
Prasert SUNTINANALERT ◽  
...  
Keyword(s):  
Serine Proteinase ◽  
Purification And Characterization ◽  
Alkaline Serine Proteinase

scholarly journals Mouse macrophage elastase. Purification and characterization as a metalloproteinase

1981 ◽  
Vol 193 (2) ◽  
pp. 589-605 ◽  
Author(s):  
M J Banda ◽  
Z Werb
Keyword(s):  
Culture Medium ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Serine Proteinase ◽  
Peritoneal Macrophages ◽  
Serine Proteinases ◽  
Endogenous Inhibitor ◽  
Purification And Characterization ◽  
Predominant Form ◽  
Mouse Peritoneal Macrophages

Macrophage elastase was purified from tissue-culture medium conditioned by inflammatory mouse peritoneal macrophages. Characterized as a secreted neutral metalloproteinase, this enzyme was shown to be catalytically and immunochemically distinct from the mouse pancreatic and mouse granulocyte elastases, both of which are serine proteinases. Inhibition profiles, production of nascent N-terminal leucine residues and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis of degraded elastin indicated that macrophage elastase is an endopeptidase, with properties of a metalloproteinase, rather than a serine proteinase. Macrophage elastase was inhibited by alpha 2-macroglobulin, but not by alpha 1-proteinase inhibitor. Macrophage elastase was resolved into three chromatographically distinct forms. The predominant form had mol.wt. 22 000 and was purified 4100-fold. Purification of biosynthetically radiolabelled elastase indicated that this form represented less than 0.5% of the secreted protein of macrophages. Approx. 800% of the starting activity was recovered after purification. Evidence was obtained for an excess of an endogenous inhibitor masking more than 80% of the secreted activity.

Purification and Characterization of Serine Proteinase from a Halophilic Bacterium,Filobacillussp. RF2-5

2005 ◽  
Vol 69 (1) ◽  
pp. 38-44 ◽  
Author(s):  
Kazumi HIRAGA ◽  
Yasushi NISHIKATA ◽  
Sirilak NAMWONG ◽  
Somboon TANASUPAWAT ◽  
Katsumi TAKADA ◽  
...  
Keyword(s):  
Serine Proteinase ◽  
Halophilic Bacterium ◽  
Purification And Characterization

scholarly journals Purification and characterization of a fibrinogenolytic serine proteinase fromAspergillus fumigatusculture filtrate

FEBS Letters ◽  
1992 ◽  
Vol 308 (1) ◽  
pp. 65-69 ◽  
Author(s):  
Gérald Larcher ◽  
Jean-Philippe Bouchara ◽  
Véronique Annaix ◽  
Françoise Symoens ◽  
Dominique Chabasse ◽  
...  
Keyword(s):  
Serine Proteinase ◽  
Purification And Characterization

scholarly journals Purification and characterization of the heat-stable serine proteinase from Thermomonospora fusca YX

1987 ◽  
Vol 246 (2) ◽  
pp. 511-517 ◽  
Author(s):  
T W Gusek ◽  
J E Kinsella
Keyword(s):  
Thermal Stability ◽  
Ionic Strength ◽  
Serine Proteinase ◽  
Maximum Activity ◽  
Exchange Chromatography ◽  
Cation Exchange Chromatography ◽  
Purification And Characterization ◽  
Thermomonospora Fusca ◽  
Heat Stable

The proteinase secreted from Thermomonospora fusca YX grown on cellulose was purified by (NH4)2SO4 fractionation and cation-exchange chromatography. The isolated proteinase readily hydrolysed several proteins and demonstrated activity towards casein from 35 to 95 degrees C (at pH 8.0) with maximum activity at 80 degrees C. It exhibited broad pH and ionic-strength optima centered at pH 9.0 and 0.2 M-NaCl respectively, and it retained high activity in the presence of 2% (w/v) SDS, 20 mM-dithiothreitol and 1.0 M-NaCl. The proteinase, which was fully inhibited by phenylmethanesulphonyl fluoride, had an Mr of 14,500 and an isoelectric point at 9.21. A measurement of proteinase thermal stability demonstrated a T50% (15 min) of 85 degrees C at pH 4.5.

Purification and characterization of a halotolerant serine proteinase from thermotolerant Bacillus licheniformis RKK-04 isolated from Thai fish sauce

2010 ◽  
Vol 86 (6) ◽  
pp. 1867-1875 ◽  
Author(s):  
Yoichi Toyokawa ◽  
Hiroaki Takahara ◽  
Alissara Reungsang ◽  
Masakazu Fukuta ◽  
Yuki Hachimine ◽  
...  
Keyword(s):  
Bacillus Licheniformis ◽  
Serine Proteinase ◽  
Fish Sauce ◽  
Purification And Characterization
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