Conservation of functional site structure across different membrane transport protein families

A - Papers appearing in refereed journals

Mullins, J. G. L., Knight, G. L., Sarakinou, K. S. and Antoniw, J. F. 2000. Conservation of functional site structure across different membrane transport protein families. Biochemical Society Transactions. 28 (1), p. A40.

AuthorsMullins, J. G. L., Knight, G. L., Sarakinou, K. S. and Antoniw, J. F.
Abstract

Beuuveriu hsim, pwn in potato dextrose broth and measured their activity by their ability to agglutinate human erythrocytes. The lectins were purified by ion-exchange chromatography and affinity methods to give preparations that gave a single band in SDS-PAGE. Basic characterization has been carried out. The X. polvtnorphu lectin shows specificity for lactose and the B. hassiunu lectin for N-acetyl-Dglucosamine; both lectins have subunit masses of approx. 17 kDa. The N-terminal of each protein was determined. The X. pnlvmrphu lectin shows similarities with the galectin isolated from the fungus Coprims cinereus and is, possibly, a new member of the galectin family. B. hassiaM is insecticidal and it is interesting to note that its lectin has sequence homology with the N-acetyl-D-glucosamine-specific lectin from the fungus

Year of Publication2000
JournalBiochemical Society Transactions
Journal citation28 (1), p. A40
Funder project or code000
ISSN0300-5127
PublisherPortland Press Ltd

Permalink - https://repository.rothamsted.ac.uk/item/883q0/conservation-of-functional-site-structure-across-different-membrane-transport-protein-families

29 total views
0 total downloads
0 views this month
0 downloads this month