Purification and characterization of SDS stable protease from Bacillus safensis strain CK

AbstractThe chitinase producing bacterial strain was isolated from the vermicompost amended site of Mehsana district of Gujarat, India, and identified as Bacillus safensis MBCU6 using 16S rDNA sequencing. The chitinase was purified by ammonium sulfate precipitation followed by diethylaminoethanol sepharose CL-6B column chromatography. The purified enzyme could be demonstrated as a single band on sodium dodecyl sulfate polyacryalamide gel electrophoresis analysis as well as clear zone on zymogram, with estimated molecular mass of 58 kDa. The optimum pH and temperature of chitinase were pH 7.0 and 60◦C, respectively. The purified chitinase exhibited high degree of antifungal activity particularly against pathogenic Macrophomina phaseolina (60%) and Rhizoctonia solani (73%) by dissolving their cell wall components. The purified enzyme could hydrolyze colloidal chitin to its oligomers. It infers that the chitinase produced by Bacillus safensis may play a significant role in the activity as a biopesticide and bioactive material production.

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Cloning, expression, purification and characterization of HSP105

Cell Biology International ◽

10.1042/cbi034s046a ◽

2010 ◽

Vol 34 (8) ◽

pp. S46-S46

Author(s):

Dong Han ◽

Huang Xu

Keyword(s):

Purification And Characterization

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Cloning and high level expression of Cynodon dactylon (Bermuda grass) pollen profilin (Cyn d 12) in Escherichia coli: purification and characterization of the allergen

Clinical & Experimental Allergy ◽

10.1046/j.1365-2222.1997.1470952.x ◽

1997 ◽

Vol 27 (11) ◽

pp. 1307-1313 ◽

Cited By ~ 2

Author(s):

J. A. ASTURIAS ◽

M. C. ARILLA ◽

N. GOMEZ-BAYON ◽

J. MARTINEZ ◽

A. MARTINEZ ◽

...

Keyword(s):

Escherichia Coli ◽

Grass Pollen ◽

Cynodon Dactylon ◽

Bermuda Grass ◽

Purification And Characterization ◽

High Level Expression ◽

Bermuda Grass Pollen ◽

D 12 ◽

High Level

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Purification and characterization of a (1 → 3)-β-?-glucan-binding protein from horseshoe crab (Tachypleus tridentatus) amoebocytes

Carbohydrate Research ◽

10.1016/s0008-6215(96)00214-5 ◽

1996 ◽

Vol 295 (1-4) ◽

pp. 103-116

Author(s):

H Tamura

Keyword(s):

Horseshoe Crab ◽

Binding Protein ◽

Purification And Characterization ◽

Tachypleus Tridentatus

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Purification and characterization of phosphoglucomutase from peas

Physiologia Plantarum ◽

10.1034/j.1399-3054.1994.920317.x ◽

1994 ◽

Vol 92 (3) ◽

pp. 479-486 ◽

Cited By ~ 1

Author(s):

Cynthia M. Galloway ◽

W. Mack Dugger

Keyword(s):

Purification And Characterization

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Purification and Characterization of Tissue-Type Plasminogen Activator in Maxillary Mucosa with Chronic Inflammation

Thrombosis and Haemostasis ◽

10.1055/s-0038-1657879 ◽

1985 ◽

Vol 54 (02) ◽

pp. 485-489 ◽

Cited By ~ 3

Author(s):

Yukiyoshi Hamaguchi ◽

Masuichi Ohi ◽

Yasuo Sakakura ◽

Yasuro Miyoshi

Keyword(s):

Plasminogen Activator ◽

Chronic Inflammation ◽

Gel Filtration ◽

Potassium Acetate ◽

Tissue Type ◽

Purification And Characterization ◽

Tissue Type Plasminogen Activator ◽

Urokinase Inhibitor ◽

Type Plasminogen Activator

SummaryTissue-type plasminogen activator (TPA) was purified from maxillary mucosa with chronic inflammation and compared with urokinase. Purification procedure consisted of the extraction from delipidated mucosa with 0.3M potassium acetate buffer (pH 4.2), 66% saturation of ammonium sulfate, zinc chelate-Sepharose, concanavalin A-Sepharose and Sephadex G-100 gel filtration chromatographies.The molecular weight of the TPA was approximately 58,000 ± 3,000. Its activity was enhanced in the presence of fibrin and was quenched by placental urokinase inhibitor, but not quenched by anti-urokinase antibody. The TPA made no precipitin line against anti-urokinase antibody, while urokinase did.All these findings indicate that the TPA in maxillary mucosa with chronic inflammation is immunologically dissimilar to urokinase and in its affinity for fibrin.

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Prothrombin Metz : Purification and Characterization of a Variant of Human Prothrombin

10.1055/s-0038-1665670 ◽

1979 ◽

Author(s):

M Ribieto ◽

J Elion ◽

D Labie ◽

F Josso

Keyword(s):

Molecular Weight ◽

Gel Electrophoresis ◽

Polyacrylamide Gel Electrophoresis ◽

Factor Xa ◽

Polyacrylamide Gel ◽

Cleavage Pattern ◽

Purification And Characterization ◽

Double Immunodiffusion ◽

The Family

For the purification of the abnormal prothrombin (Pt Metz), advantage has been taken of the existence in the family of three siblings who, being double heterozygotes for Pt Metz and a hypoprothrombinemia, have no normal Pt. Purification procedures included barium citrate adsorption and chromatography on DEAE Sephadex as for normal Pt. As opposed to some other variants (Pt Barcelona and Madrid), Pt Metz elutes as a single symetrical peak. By SDS polyacrylamide gel electrophoresis, this material is homogeneous and appears to have the same molecular weight as normal Pt. Comigration of normal and abnormal Pt in the absence of SDS, shows a double band suggesting an abnormal charge for the variant. Pt Metz exhibits an identity reaction with the control by double immunodiffusion. Upon activation by factor Xa, Pt Metz can generate amydolytic activity on Bz-Phe-Val-Arg-pNa (S2160), but only a very low clotting activity. Clear abnormalities are observed in the cleavage pattern of Pt Metz when monitored by SDS gel electrophoresis. The main feature are the accumulation of prethrombin l (Pl) and the appearance of abnormal intermediates migrating faster than Pl.

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