Table of Contents
Journal of Amino Acids
Volume 2013, Article ID 569527, 6 pages
http://dx.doi.org/10.1155/2013/569527
Research Article

Peptide Mass Fingerprinting and N-Terminal Amino Acid Sequencing of Glycosylated Cysteine Protease of Euphorbia nivulia Buch.-Ham.

1Department of Biotechnology, Faculty of Science, Post Graduate College of Science, Technology and Research, North Maharashtra University, Jalgaon, Maharashtra 425002, India
2Department of Biotechnology, Faculty of Science, Moolji Jaitha College, Jalgaon, Maharashtra 425002, India

Received 24 October 2012; Revised 30 December 2012; Accepted 30 December 2012

Academic Editor: Hieronim Jakubowski

Copyright © 2013 Shamkant B. Badgujar and Raghunath T. Mahajan. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

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.