Purification and characterization of a hemagglutinin isolated from the leaves of Chenopodium (Chenopodium amaranticolor).
Indian J Biochem Biophys
;
2001 Jun; 38(3): 186-92
Article
in English
| IMSEAR
| ID: sea-28814
ABSTRACT
A hemagglutinin was isolated and purified from the leaves of Chenopodium (Chenopodium amaranticolor) using ion-exchange chromatography and affinity chromatography on fetuin-agarose matrix. It agglutinated rabbit erythrocytes. The hemagglutinin had a native molecular mass of 58 kDa, as estimated by gel filtration and showed a single band of molecular mass of 33 kDa on SDS-PAGE. It showed hemagglutination activity over the pH range 3-12 and was found to be stable up to 70 degrees C. On isoelectrofocussing, the pI of this hemagglutinin was estimated to be 5.25. However, it was found to contain seven charge variants when isoelectrofocussing was performed in presence of 6M urea.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Protein Binding
/
Temperature
/
Time Factors
/
Chromatography, Gel
/
Chromatography, Ion Exchange
/
Plant Leaves
/
Chenopodium
/
Electrophoresis, Polyacrylamide Gel
/
Hemagglutinins
/
Hydrogen-Ion Concentration
Language:
English
Journal:
Indian J Biochem Biophys
Year:
2001
Type:
Article
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