Protein identification from the parotoid macrogland secretion of Duttaphrynus melanostictus
| Autor: | Patrick Jack Spencer, Marcela Di Giacomo Messias, Douglas Oscar Ceolin Mariano, Daniel C. Pimenta |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Proteomics Batch chromatography Asian common toad lcsh:Arctic medicine. Tropical medicine Calmodulin lcsh:RC955-962 030231 tropical medicine Duttaphrynus melanostictus Peptide Toxicology Amphibian skin secretion 03 medical and health sciences 0302 clinical medicine lcsh:RA1190-1270 lcsh:Zoology Secretion lcsh:QL1-991 Galectin Alcohol dehydrogenase lcsh:Toxicology. Poisons chemistry.chemical_classification 030102 biochemistry & molecular biology Molecular mass biology Bufonidae Infectious Diseases Histone chemistry Biochemistry biology.protein Animal Science and Zoology Parasitology |
| Zdroj: | Journal of Venomous Animals and Toxins including Tropical Diseases, Volume: 25, Article number: e20190029, Published: 19 AUG 2019 Journal of Venomous Animals and Toxins including Tropical Diseases, Vol 25 Journal of Venomous Animals and Toxins including Tropical Diseases v.25 2019 The Journal of venomous animals and toxins including tropical diseases Universidade Estadual Paulista (UNESP) instacron:UNESP |
| Popis: | Background: Bufonid parotoid macrogland secretion contains several low molecular mass molecules, such as alkaloids and steroids. Nevertheless, its protein content is poorly understood. Herein, we applied a sample preparation methodology that allows the analysis of viscous matrices in order to examine its proteins. Methods: Duttaphrynus melanostictus parotoid macrogland secretion was submitted to ion-exchange batch sample preparation, yielding two fractions: salt-displaced fraction and acid-displaced fraction. Each sample was then fractionated by anionic-exchange chromatography, followed by in-solution proteomic analysis. Results: Forty-two proteins could be identified, such as acyl-CoA-binding protein, alcohol dehydrogenase, calmodulin, galectin and histone. Moreover, de novo analyses yielded 153 peptides, whereas BLAST analyses corroborated some of the proteomic-identified proteins. Furthermore, the de novo peptide analyses indicate the presence of proteins related to apoptosis, cellular structure, catalysis and transport processes. Conclusions: Proper sample preparation allowed the proteomic and de novo identification of different proteins in the D. melanostictus parotoid macrogland secretion. These results may increase the knowledge about the universe of molecules that compose amphibian skin secretion, as well as to understand their biological/physiological role in the granular gland. |
| Databáze: | OpenAIRE |
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