Off-campus Michigan Tech users: To download campus access theses or dissertations, please use the following button to log in with your Michigan Tech ID and password: log in to proxy server
Non-Michigan Tech users: Please talk to your librarian about requesting this thesis or dissertation through interlibrary loan.
Date of Award
Master of Science in Chemistry (MS)
College, School or Department Name
Department of Chemistry
Tarun K. Dam
Two novel mannose specific lectins named Fabiolin and DIL, were purified from the storage tissues of two monocot species, using a new method known as “Capture and Release” (CARE). CARE is a method developed based on the binding properties of the targeted proteins and can be used as a general purification protocol for isolating new lectins. Fabiolin and DIL are tetrameric proteins with a subunit molecular weight of 8 kDa. At higher concentration, both lectins show hemolytic activity, whereas at lower concentration, they agglutinate red blood cells. Hemagglutination inhibition, quantitative precipitation and calorimetric studies show that these lectins strongly interact with yeast high mannose glycoprotein invertase and yeast surface mannan. These interactions suggest that Fabiolin and DIL can potentially act as endogenous antifungal agents in order to protect the plants. In addition, they have the potential to modulate invertasemediated metabolic pathways that regulate ATP production, development, and synthesis of starch and secondary metabolites in plants.
Fueri, Ashli L., "CHARACTERIZATION OF TWO NOVEL MONOCOT MANNOSE BINDING LECTINS PURIFIED BY ‘CAPTURE AND RELEASE’ METHOD", Master's Thesis, Michigan Technological University, 2013.