Although work on the prolamins of pearl millet (Pennisetum glaucum) has revealed partial amino acid sequences for several alcohol-soluble storage proteins (Marcellino et al. 2002) the genes encoding them have not yet been isolated. We constructed a cDNA library from developing P. glaucum seed tissue and screened it using maize zein gene probes to isolate several α-prolamin-like gene sequences. The proteins encoded by these genes generally fall into two size classes: 20.6kD and 27.1kD, which we call the 21kD and 27kD pennisetins. Both proteins are similar in composition and sequence to α-prolamins from maize, sorghum and Coix. Protein bodies that appear as occlusions within the rough ER of P. glaucum endosperm cells are also very similar in size and shape to maize and sorghum protein bodies. The SDS-PAGE gel of the alcohol soluble protein fraction shows two distinct bands in the region corresponding to the 19kD and 22kD of maize α-zein. Both classes of pennisetins appear to be more similar to the 19kD α-zein of maize than to the 22-kD α-zein judging from sequence homology and maize antibody binding. Phylogenetic reconstruction suggests that P. glaucum may have branched from maize prior to the gene duplication which created the 19kD and 22kD α-zein families.

Lectins and hemagglutinins are carbohydrate binding proteins present in a diversity of organisms including humans, vertebrate and invertebrate animals, plants, fungi, and bacteria. They are usually the abundant storage proteins in leguminous plants. They display a host of biological activities such as antitumor, antifungal, antiviral, insecticidal, and antibacterial activities. / The biological properties of isolated proteins, including hemagglutinating, antifungal, anti-tumor and HIV-1 reverse transcriptase inhibitory activities, were examined. Their biochemical and biological properties were compared with other purified proteins. / The seeds contain an abundance of proteins, some of which are storage proteins but may play a role of protection from pathogenic microbes and phytophagous insects. Antifungal peptides/proteins, antiviral proteins, ribosome-inactivating proteins, proteinase inhibitors, chitinases, proteinases, and defensins, are some examples of the myriad of seed proteins. The aforementioned proteins are collectively called plant defense proteins in view of their antipathogenic activities. These antifungal proteins exhibit a wide range of molecular masses and amino acid sequences. / Two lectins with potentially exploitable activities were purified from Capparis spinosa seeds and Hibiscus mutabilis seeds, respectively. A hemagglutinin was isolated from Phaselous vulgaris , cultivar "French bean 35", and detailed apoptotic pathway in breast cancer cells, MCF-7 cells, was investigated. A novel dimeric beta-lactoglobulin-like antifungal protein and an antifungal amidase were purified from Passiflora edilus seeds and Peltophorum pterocarpum, respectively. / Lam, Sze Kwan. / Adviser: Tsi Bun Ng. / Source: Dissertation Abstracts International, Volume: 72-04, Section: B, page: . / Thesis (Ph.D.)--Chinese University of Hong Kong, 2010. / Includes bibliographical references (leaves 188-204). / Electronic reproduction. Hong Kong : Chinese University of Hong Kong, [2012] System requirements: Adobe Acrobat Reader. Available via World Wide Web. / Electronic reproduction. Ann Arbor, MI : ProQuest Information and Learning Company, [200-] System requirements: Adobe Acrobat Reader. Available via World Wide Web. / Abstract also in Chinese.