Proteomics

Dataset Information

0

Analysis of C.monile venom peptides.


ABSTRACT: Mass Spectrometric Characterisation of conophysin/ conopressin.

INSTRUMENT(S): maXis

ORGANISM(S): Conus Monile

TISSUE(S): Venom Duct, Epithelial Cell

SUBMITTER: P Balaram  

LAB HEAD: Prof.P.Balaram, Molecular Biophysics Unit

PROVIDER: PXD012899 | Pride | 2020-02-21

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
569-25-E.mgf Mgf
575-77-KE.mgf Mgf
576-25-KE.mgf Mgf
753-31-E.mgf Mgf
819-34-K.mgf Mgf
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Publications

Cone snail analogs of the pituitary hormones oxytocin/vasopressin and their carrier protein neurophysin. Proteomic and transcriptomic identification of conopressins and conophysins.

Kumar Sanjeev S   Vijayasarathy M M   Venkatesha M A MA   Sunita P P   Balaram P P  

Biochimica et biophysica acta. Proteins and proteomics 20200210 5


Transcriptomic analysis of cone snail venom duct tissue has permitted the identification of diverse conopressin/conophysin precursor sequences from seven distinct Conus species. Multiple precursor isoforms are present in C.monile, C.lividus and C.loroisii. Aqueous extracts of the venom duct tissue from C.monile yield a band, at ~ 15-20 kDa on SDS-PAGE. In-gel trypsin digestion, followed by mass spectrometry establishes the presence of two distinct conopressin/conophysin isoforms that differ at p  ...[more]

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