Application of selective extraction and reverse phase chromatography with three detectors – PAD, FLD and ESI MS for characterization of platinum metabolites and identification of phytochelatins in Sinapis alba L. tissues

2017 ◽  
Vol 132 ◽  
pp. 198-204 ◽  
Author(s):  
Joanna Kowalska ◽  
Katarzyna Kińska ◽  
Magdalena Biesaga ◽  
Monika Asztemborska
Keyword(s):  
Selective Extraction ◽  
Sinapis Alba ◽  
Reverse Phase ◽  
Reverse Phase Chromatography ◽  
Esi Ms ◽  
Sinapis Alba L

scholarly journals Characterization of five new low-molecular-mass trypsin inhibitors from white mustard (Sinapis alba L.) seed

2000 ◽  
Vol 267 (21) ◽  
pp. 6486-6492 ◽  
Author(s):  
Margherita Ruoppolo ◽  
Angela Amoresano ◽  
Piero Pucci ◽  
Stefano Pascarella ◽  
Fabio Polticelli ◽  
...  
Keyword(s):  
Molecular Mass ◽  
Sinapis Alba ◽  
Trypsin Inhibitors ◽  
White Mustard ◽  
Sinapis Alba L

Isolation and characterization of a trypsin inhibitor from white mustard (Sinapis alba L.)

1985 ◽  
Vol 33 (5) ◽  
pp. 784-789 ◽  
Author(s):  
Enea Menegatti ◽  
Sandro Palmieri ◽  
Peter Walde ◽  
Pier Luigi Luisi
Keyword(s):  
Trypsin Inhibitor ◽  
Sinapis Alba ◽  
White Mustard ◽  
Isolation And Characterization ◽  
Sinapis Alba L

Characterization of Glutamine Synthetase of Roots, Etiolated Cotyledons and Green Leaves from Sinapis alba (L.)

1986 ◽  
Vol 41 (7-8) ◽  
pp. 712-716 ◽  
Author(s):  
Remigius Manderscheid ◽  
Aloysius Wild
Keyword(s):  
Glutamine Synthetase ◽  
Crude Extract ◽  
Substrate Binding ◽  
Sinapis Alba ◽  
Kinetic Properties ◽  
Temperature Optimum ◽  
Ph Optimum ◽  
Green Leaves ◽  
Sinapis Alba L

Abstract Glutamine synthetase of roots, etiolated cotyledons and green leaves from mustard plants cannot all clearly be separated by DEAE-Sephacel chromatography. However, the enzyme of the roots, etiolated cotyledons and green leaves, respectively, differed in the kinetic properties deter­mined in the crude extract. The root enzyme showed a pH-optimum of about 6.9, a Km value of 3 mᴍ for glutamate and a temperature optimum at 48 °C. Glutamine synthetase of etiolated cotyledons possessed a Km for glutamate of 6 or 12 mᴍ, depending on the dithioerythritol con­centration in the homogenisation buffer and a temperature optimum at 46 °C. The enzyme of green leaves was characterized by a temperature optimum at 40 °C, a pH-optimum at about 7.4 and a low glutamate affinity with positive cooperative substrate binding. Based on isolation of chloroplasts and identification of glutamine synthetase the enzyme of green leaves seems to be the chloroplastic form. This enzyme was purified by DEAE-Sephacel, hydroxylapatite and Sephacryl S-300 chromatography. Affinity for glutamate and MgSO4 of the purified enzyme differed from that found in the crude extract. The function of the different isoenzymes is discussed.

The Production, Optimization, and Characterization of Biodiesel from a Novel Source: Sinapis alba L

2013 ◽  
Vol 11 (3) ◽  
pp. 280-291 ◽  
Author(s):  
Shazia Sultana ◽  
Aneela Khalid ◽  
Mushtaq Ahmad ◽  
Ahmad Abdullah Zuhairi ◽  
Lee Keat Teong ◽  
...  
Keyword(s):  
Sinapis Alba ◽  
Production Optimization ◽  
Sinapis Alba L

Characterization of Enterobacter intermedius MH8b and its use for the enhancement of heavy metals uptake by Sinapis alba L.

2013 ◽  
Vol 63 ◽  
pp. 1-7 ◽  
Author(s):  
T. Płociniczak ◽  
A. Sinkkonen ◽  
M. Romantschuk ◽  
Z. Piotrowska-Seget
Keyword(s):  
Heavy Metals ◽  
Sinapis Alba ◽  
Sinapis Alba L ◽  
Heavy Metals Uptake
Sign in / Sign up

Export Citation Format

Share Document