%0 Journal Article
%T Peptide Mass Fingerprinting and N-Terminal Amino Acid Sequencing of Glycosylated Cysteine Protease of Euphorbia nivulia Buch.-Ham.
%A Shamkant B. Badgujar
%A Raghunath T. Mahajan
%J Journal of Amino Acids
%D 2013
%I Hindawi Publishing Corporation
%R 10.1155/2013/569527
%X A new cysteine protease named Nivulian-II has been purified from the latex of Euphorbia nivulia Buch.-Ham. The apparent molecular mass of Nivulian-II is 43670.846 Da (MALDI TOF/MS). Peptide mass fingerprint analysis revealed peptide matches to Maturase K (Q52ZV1_9MAGN) of Banksia quercifolia. The N-terminal sequence (DFPPNTCCCICC) showed partial homology with those of other cysteine proteinases of biological origin. This is the first paper to characterize a Nivulian-II of E. nivulia latex with respect to amino acid sequencing. 1. Introduction Proteases are enzymes which potentially hydrolyze anything that contains peptide bond, from a dipeptide up to a large protein, containing thousands of amino acids and, thus, it comprises a group of hydrolases that are the most relevant in technological terms. Proteolytic enzymes have been the subject of intensive studies for a number of years because proteases have great therapeutic and industrial applications as well [1]. Peptidases in which the nucleophile that attacks the scissile peptide bond is the sulfhydryl group of a cysteine residue are known as cysteine-type peptidase. Many plant proteases have been isolated from the lattices and most of them belong to this catalytic type. Plant cysteine proteases belong to a class which has been widely studied over the years. These enzymes are also used in industries owing to their high stability [2]. Plant cysteine proteases play a major role in the intracellular and extracellular process such as development and ripening of fruits, degradation of storage proteins in germinating seeds, activation of proteins, and degradation of defective proteins [3]. Besides, latex proteases are also involved in the protection of the plants against predator attack [4]. Many researchers have isolated and characterized the plant origin proteases of diverse group. Euphorbia nivulia Buch.-Ham. is a wild, thorny, xerophytic, succulent plant, found in boundaries of the agricultural field and also in dry barren areas. The secretion of milky juice is a characteristic property of this plant. Phytochemical studies have led to the isolation of ingol diterpenes (3-acetyl-8-methoxyl-7-angolyl-12-hydroxylingol; 3,12-diacetyl-7-hydroxy-8-methoxylingol; 3,12-diacetyl-7-angolyl-8-hydroxylingol; 3,12-diacetyl-8-benzoylingol; and 3,12-diacetyl-7-benzoyl-8-nicotinylingol) along with three macrocyclic ingol diterpenes derivatives (3,7,12-triacetyl-8-benzoylingol; 3,12-diacetyl-7-angeloyl-8-methoxyingol; and 7-angeloyl-12-acetyl-8-methoxyingol) [5]. The latex of E. nivulia has been cited for its antioxidant,
%U http://www.hindawi.com/journals/jaa/2013/569527/