Deakin University
Browse

File(s) under permanent embargo

A kinetically stable plant subtilase with unique peptide mass fingerprints and dimerization properties

journal contribution
posted on 2009-01-01, 00:00 authored by Subhash Chandra Yadav, M V Jagannadham, S Kundu
Milin, a potent molluscicide from the latex of Euphorbia milii, holds promise in medicinal biochemistry. Electrophoresis, size exclusion chromatography, mass spectrometry and other biochemical characteristics identify milin as a homodimeric, plant subtilisin-like serine protease, the first of its kind. The subunits of milin are differentially glycosylated affecting dimer association, solubility and proteolytic activity. The dimeric dissociation is SDS-insensitive and strongly temperature dependent but does not appear to be linked by disulfide bridges. N-terminal sequence of acid hydrolyzed peptide fragments shows no homology to known serine protease. Peptide mass fingerprinting and de novo sequencing of the tryptic fragments also did not identify putative domains in the protein. Milin seems to be a novel plant enzyme with subunit association partly similar to human herpes virus serine proteases and partly to penicillin binding proteins. Its behaviour on SDS-PAGE gels and other properties is like "kinetically stable" proteins. Such subunit association and properties might play a critical role in its physiological function and in controlling Schistosomiasis.

History

Journal

Biophysical chemistry

Volume

139

Issue

1

Pagination

13 - 23

Publisher

Elsevier BV

Location

Amsterdam, The Netherlands

ISSN

0301-4622

eISSN

1873-4200

Language

eng

Publication classification

C1.1 Refereed article in a scholarly journal

Copyright notice

2008, Elsevier B.V.