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Identification and characterization of Euphorbia nivulia latex proteins
Shamkant B Badgujar1, Raghunath T Mahajan2
1Department of Biochemistry, National Institute for Research in Reproductive Health, ICMR, Jehangir Merwanji Street, Parel, Mumbai 400 012, Maharashtra, India; Faculty of Science, Department of Biotechnology, Moolji Jaitha College, North Maharashtra University, Jalgaon 425 002, Maharashtra, India.
Abstract:
The protein profile of latex of Euphorbia nivulia Buch.-Ham. is established. Three new proteins viz., Nivulian-I, II and III have been purified to homogeneity from the latex. The relative molecular masses of Nivulian-I, II and III are 31,486.985, 43,670.846 and 52,803.470 Da respectively. Nivulian-I is a simple type of protein while Nivulian-II and III are glycoproteins. Peptide mass fingerprint analysis revealed peptides of these proteins match with Tubulin alpha-1 chain of Eleusine indica, Maturase K of Banksia quercifolia and hypothetical protein of Zea mays respectively. Tryptic digestion profile of Nivulian-I, II and III, infer the exclusive nature of latex origin proteins and may be new and are additive molecules in the dictionaries of phytoproteins or botany. This is the first of its kind, regarding characterization and validation of Nivulian-I, II and III with respect to peptide sequencing.
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