Purification and characterization of a novel short-chain insecticidal toxin with two disulfide bridges from the venom of the scorpion Liocheles australasiae

Toxicon ◽  
2007 ◽  
Vol 50 (6) ◽  
pp. 861-867 ◽  
Author(s):  
Nobuto Matsushita ◽  
Masahiro Miyashita ◽  
Atsushi Sakai ◽  
Yoshiaki Nakagawa ◽  
Hisashi Miyagawa
Keyword(s):  
Short Chain ◽  
Disulfide Bridges ◽  
Purification And Characterization ◽  
Insecticidal Toxin

Purification and Characterization of Two Polymorphic Variants of Short Chain Acyl-CoA Dehydrogenase Reveal Reduction of Catalytic Activity and Stability of the Gly185Ser Enzyme†

Biochemistry ◽  
2002 ◽  
Vol 41 (37) ◽  
pp. 11126-11133 ◽  
Author(s):  
Tien V. Nguyen ◽  
Charles Riggs ◽  
Dusica Babovic-Vuksanovic ◽  
Yong-Sung Kim ◽  
John F. Carpenter ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Short Chain ◽  
Purification And Characterization ◽  
Chain Acyl ◽  
Polymorphic Variants

scholarly journals Purification and Characterization of a Novel Pumpkin Short-Chain Acyl-Coenzyme A Oxidase with Structural Similarity to Acyl-Coenzyme A Dehydrogenases

2000 ◽  
Vol 123 (1) ◽  
pp. 327-334 ◽  
Author(s):  
Luigi De Bellis ◽  
Silvia Gonzali ◽  
Amedeo Alpi ◽  
Hiroshi Hayashi ◽  
Makoto Hayashi ◽  
...  
Keyword(s):  
Coenzyme A ◽  
Structural Similarity ◽  
Short Chain ◽  
Purification And Characterization ◽  
Chain Acyl ◽  
Acyl Coenzyme A

scholarly journals Purification and Characterization of a Novel Insecticidal Toxin, μ-sparatoxin-Hv2, from the Venom of the Spider Heteropoda venatoria

Toxins ◽  
2018 ◽  
Vol 10 (6) ◽  
pp. 233
Author(s):  
Zhen Xiao ◽  
Yunxiao Zhang ◽  
Jiao Zeng ◽  
Songping Liang ◽  
Cheng Tang ◽  
...  
Keyword(s):  
Purification And Characterization ◽  
Insecticidal Toxin

scholarly journals Purification and characterization of a new xylanase (xylanase B) produced by Streptomyces lividans 66

1990 ◽  
Vol 267 (1) ◽  
pp. 45-50 ◽  
Author(s):  
D Kluepfel ◽  
S Vats-Mehta ◽  
F Aumont ◽  
F Shareck ◽  
R Morosoli
Keyword(s):  
Streptomyces Lividans ◽  
Genetically Engineered ◽  
Cross Reaction ◽  
Short Chain ◽  
Purification And Characterization ◽  
Specific Antibodies ◽  
Hydrolysis Products

A new extracellular xylanase produced by Streptomyces lividans 66 was isolated from a genetically engineered clone of that strain. This enzyme, named xylanase B, has an Mr of 31,000 and acts specifically on xylan as an endo-type xylanase producing short-chain xylo-oligosaccharides. The activity is optimal at pH 6.5 and at a temperature of 55 degrees C, which is similar to that of the previously characterized xylanase A. Xylanase B is glycosylated and has a pI of 8.4; its Km and Vmax. values are 3.71 mg/ml and 1.96 mmol/mg of enzyme respectively. Specific antibodies raised against xylanase A show no cross-reaction with xylanase B; however, the anti-(xylanase B) antibodies react slightly with xylanase A. A comparison of the hydrolysis products obtained from oat-spelts xylan with both enzymes show that xylanase A preferentially degrades short-chain oligo-xylosides, whereas xylanase B acts on the longer, water-insoluble, molecules.

scholarly journals Purification and characterization of the short-chain alkylsulphatase of coryneform B1a

1994 ◽  
Vol 304 (3) ◽  
pp. 937-943 ◽  
Author(s):  
P J Matts ◽  
G F White ◽  
W J Payne
Keyword(s):  
Butyric Acid ◽  
Deae Cellulose ◽  
Short Chain ◽  
Purification And Characterization ◽  
Streptomycin Sulphate ◽  
Competitive Inhibitors ◽  
Specificity Constant ◽  
A Subunit ◽  
Ester Linkage

Using a combination of streptomycin sulphate precipitation, and DEAE-cellulose and butyl-agarose chromatography, an alkylsulphatase active towards short-chain alkyl sulphates has been purified approx. 70-fold from extracts of coryneform B1a grown on butyl-1-sulphate. The enzyme protein is dimeric with a subunit molecular mass of 77.6 kDa, has an isoelectric point of pI 7.2, and converts butyl-1-sulphate stoichiometrically into butan-1-ol and inorganic sulphate. Stoichiometric incorporation of 18O from H2(18)O into sulphate during the reaction showed that enzymic hydrolysis occurred at the O-S bond of the C-O-S ester linkage. The enzyme was active on C3-C7 linear primary alkyl sulphates but not on higher (C8,9) or lower (C1,2) homologues, although the latter pair were competitive inhibitors. The specificity constant (kcat./Km) was highest for pentyl sulphate (Km 1.89 +/- 0.38 mM; kcat. 6.86 +/- 0.52 s-1) and decreased for higher and lower homologues. No activity was detected towards C3-C9 racemic alkyl-2-sulphates, D- or L-enantiomers of butyl-2-sulphate, the symmetrical secondary alkyl sulphates pentyl-3-sulphate, heptyl-4-sulphate, nonyl-5-sulphate, C1-C8 alkane sulphonates, choline sulphate, or butyric acid-4-sulphate; none of these compounds (except the symmetrical esters and butyric acid-4-sulphate, which were not tested) was demonstrably inhibitory. The enzyme was compared with other alkylsulphatases in terms of substrate specificity and mode of action.

Cloning, expression, purification and characterization of HSP105

2010 ◽  
Vol 34 (8) ◽  
pp. S46-S46
Author(s):  
Dong Han ◽  
Huang Xu
Keyword(s):  
Purification And Characterization
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