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Lectin status, protein contents and ammonium assimilating
enzymatic activity of two indigenous cultivars of mulberry
species, Morus alba and Morus nigra
Muhammad Zahoor*, Zakia Javaid, Muhammad Ali, Saleem Khan,
Farhad Ali and Zahoor A. Swati
Institute
of Biotechnology and Genetic Engineering, NWFP Agricultural
University Peshawar, Pakistan.
*Corresponding author. E-mail:
mzkhaans@yahoo.com.
Accepted
16 March, 2009 |
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The
studies were carried out with plantlets of two indigenous
cultivars of mulberry species Morus alba and Morus
nigra grown in soil less cultures, where extracts from
roots, shoots, leaves, and reproductive organs were
determined for protein content, agglutination of human
erythrocytes and the activity of the ammonium assimilatory
enzyme glutamine synthetase. M. nigra and M. alba
extracts contained potent phytoagglutinins in various
tissues with highest contents in M. nigra. The
leaves and roots of both species of mulberry were used to
determine the glutamine synthetase activity and high level
of activity was found in both tissues. The glutamine
synthetase enzymatic activity was higher in roots (1.37
µmol.gfw-1.min-1). The extract from
all tissues of both species were used to determine the total
protein contents and proteins found higher in the leaves
(2.129 µg/gfw in M. nigra and 0.973 µg/gfw in M.
alba).
Key
words:
Lectins, GS Assay, ammonium assimilation, mulberry species,
phytoagglutanins. |
