Proteomic analysis of the venom of Heterometrus longimanus (Asian black scorpion)

Abstract

Venoms have evolved over millions of years into potent cocktails of bioactive peptides and proteins. These compounds can be of great value to the pharmaceutical industry for numerous clinical applications. In this study, a novel proteomic - bioinformatic approach was utilised, where chromatography followed by gel electrophoresis was utilised to separate the venom peptides/proteins of Heterometrus longimanus (Asian black scorpion). Purified peptides were analysed by tandem mass spectrometry, de novo sequenced and then homology matched against known peptides in the Swiss-Prot protein database. Numerous potentially biologically active peptide matches were discovered, and a simple scoring system applied to putatively assign functions to the peptides. As a validation of this approach, the functional composition of the experimentally derived proteome is similar to that of other scorpions, and contains a potent mix of toxins, antimicrobials and ionic channel inhibitors.

Proteomic Analysis of a 14.2 kDa Protein Isolated from Bali Cattle(Bos Sondaicus/Javanicus)Saliva Using Single Dimension Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis and Matrix-Assisted Laser Desorption Ionization Time-of-Flight Tandem Mass Spectrometer

“…Peptides were extracted according to standard techniques (Bringans et al, 2008) and analysed by MALDI TOF/TOF mass spectrometer using a 5800 Proteomics Analyzer (AB Sciex, Framingham, MA, USA). Spectra were analysed to identify protein of interest using Mascot sequence matching software (Matrix Science, Boston, MA, USA) with Ludwig NR Database.…”

Unique diversity of the venom peptides from the scorpion Androctonus bicolor revealed by transcriptomic and proteomic analysis

“…Mass spectrometry (MS) was performed as described previously [18,40]. Venom peptides were reduced with dithiothreitol (DTT) and alkylated with iodoacetamide (IAA).…”

Muscle Proteomics of the Indian Major Carp Catla (Catla catla, Hamilton)

“…In the present study, out of the 10 glycolytic enzymes (6/10), namely, aldolase (C-114), triose phosphate isomerase (C- 23,24,25,112,113), GAPDH (C-120), phosphoglycerate kinase (C-39, 82), enolase (C-78, 84, 95, 97, 98, 99, 101, 115, 116, CM-162) and pyruvate kinase (C-41, 44, 86) have been identified and they represent 22 number of spots on the catla muscle proteome (Table 2 and Figure 3; Supporting Information Figure S1). Lactate dehydrogenase (C-119), the enzyme involved in anaerobic glycolysis, converting pyruvate to lactate, has also been identified.…”

“…The resulting peptides were extracted following standard techniques [24] by two 20-min incubations with 10-20 µL ACN containing 1% TFA, depending on the size of the gel piece. The resulting tryptic peptide extract was dried by rotary evaporation and stored at -20°C for further analysis by MS.…”