Partial Proteomics Analysis of Montivipera raddei Venom Partial proteomics of Montivipera raddei venom
Trends in Peptide and Protein Sciences,
Vol. 8 No. 1 (2023),
24 December 2023
,
Page 1-5 (e2)
https://doi.org/10.22037/tpps.v8i1.41610
Abstract
The snake venom is a potent source of a variety of drugs and therapeutic components. This study aimed to isolate and characterize some of proteins in Montivipera raddei venom. The protein bands and spots obtained by SDS-PAGE and two-dimensional electrophoresis were analyzed. The separated protein spots based on isoelectric point and molecular weight were scattered in the 15 to 66 kDa ranges and pI from 5 to 8. Six proteins was more extensively characterized by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF/TOF) analysis. These characterized proteins included Zinc metalloproteinase-disintegrin-like ecarin, L-amino-acid oxidase, metalloproteinase kistomin, Thiamine-monophosphate kinase, Ancrod, Acidic phospholipase A2.
HIGHLIGHTS
- Identification of several proteins from Montivipera raddei venom.
- Characterization of the six high concentrated proteins by MALDI-TOF/TOF spectroscopy in venom.
- Zinc metalloproteinase-disintegrin-like ecarin, L-amino-acid oxidase, metalloproteinase kistomin, Thiamine-monophosphate kinase, Ancrod, Acidic phospholipase A2 were identified in venom of Montivipera raddei.
- 2D-electrophoresis
- Mass spectroscopy
- Montivipera raddei
- Proteomics
- Venom
How to Cite
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