Ontology highlight
ABSTRACT:
INSTRUMENT(S): Synapt MS
ORGANISM(S): Lachesis Muta
TISSUE(S): Venom
SUBMITTER: Alexandre Keiji Tashima
LAB HEAD: Alexandre Keiji Tashima
PROVIDER: PXD045732 | Pride | 2023-10-23
REPOSITORIES: Pride
Action | DRS | |||
---|---|---|---|---|
20191220_LM1_Lucas_DDA_001.mzML | Mzml | |||
20191220_LM1_Lucas_DDA_001.raw.zip | Raw | |||
20191220_LM1_Lucas_DDA_002.mzML | Mzml | |||
20191220_LM1_Lucas_DDA_002.raw.zip | Raw | |||
20191220_LM1_Lucas_MSE_001.mzML | Mzml |
Items per page: 1 - 5 of 30 |
Biochemical and biophysical research communications 20231006
Snake venoms are known to be major sources of peptides with different pharmacological properties. In this study, we comprehensively explored the venom peptidomes of three specimens of Lachesismuta, the largest venomous snake in South America, using mass spectrometry techniques. The analysis revealed 19 main chromatographic peaks common to all specimens. A total of 151 peptides were identified, including 69 from a metalloproteinase, 58 from the BPP-CNP precursor, and 24 from a l-amino acid oxidas ...[more]