|| Checking for direct PDF access through Ovid
The soluble venom from the scorpion Tityus metuendus was characterized by various methods. In vivo experiments with mice showed that it is lethal. Extended electrophysiological recordings using seven sub-types of human voltage gated sodium channels (hNav1.1 to 1.7) showed that it contains both α- and β-scorpion toxin types. Fingerprint analysis by mass spectrometry identified over 200 distinct molecular mass components. At least 60 sub-fractions were recovered from HPLC separation. Five purified peptides were sequenced by Edman degradation, and their complete primary structures were determined. Additionally, three other peptides have had their N-terminal amino acid sequences determined by Edman degradation and reported. Mass spectrometry analysis of tryptic digestion of the soluble venom permitted the identification of the amino acid sequence of 111 different peptides. Search for similarities of the sequences found indicated that they probably are: sodium and potassium channel toxins, metalloproteinases, hyaluronidases, endothelin and angiotensin-converting enzymes, bradykinin-potentiating peptide, hypothetical proteins, allergens, other enzymes, other proteins and peptides.Venom from T. metuendus scorpion was separated and a complete fingerprint of components were identified by mass spectrometry.Five peptides were fully sequenced by Edman degradation and mass spectrometry analyses.Various peptides were sequenced at the N-terminal region by Edman degradation.Physiological action of whole soluble venom on 7 sub-types of Na+-channels were performed by patch clamp techniques.A total of 111 tryptic digested peptides from soluble venom were sequenced by mass spectrometry and identified.