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

Author:

Badgujar Shamkant B.12,Mahajan Raghunath T.2

Affiliation:

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

2. Department of Biotechnology, Faculty of Science, Moolji Jaitha College, Jalgaon, Maharashtra 425002, India

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.

Publisher

Hindawi Limited

Subject

Molecular Biology,Biochemistry,Molecular Biology,Biochemistry

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