Inhibitory properties of the anti-bothropic complex from Didelphis albiventrisserum on toxic and pharmacological actions of metalloproteases and myotoxins from bothrops asper venom11Abbreviations:SVMPs, snake venom metalloproteases; ABC, anti-bothropic complex from Didelphis albiventrisserum; DA43, 43-kDa subunit of anti-bothropic complex from D. albiventrisserum; DA45, 45-kDa subunit of anti-bothropic complex from D. albiventrisserum; MHD, dose able to induce a hemorrhagic lesion of 10 mm diameter; BaP1, basic hemorrhagic metalloprotease from Bothrops aspervenom; BaH4, acidic hemorrhagic metalloprotease from B. aspervenom; Basp-I, myotoxin I from B. aspervenom; Basp-II, myotoxin II from B. aspervenom; and Basp-III, myotoxin III from B. aspervenom.

MLA

Trento, Edilson P., et al. “Inhibitory Properties of the Anti-Bothropic Complex from Didelphis Albiventrisserum on Toxic and Pharmacological Actions of Metalloproteases and Myotoxins from Bothrops Asper Venom11Abbreviations:SVMPs, Snake Venom Metalloproteases; ABC, Anti-Bothropic Complex from Didelphis Albiventrisserum; DA43, 43-KDa Subunit of Anti-Bothropic Complex from D. Albiventrisserum; DA45, 45-KDa Subunit of Anti-Bothropic Complex from D. Albiventrisserum; MHD, Dose Able to Induce a Hemorrhagic Lesion of 10 Mm Diameter; BaP1, Basic Hemorrhagic Metalloprotease from Bothrops Aspervenom; BaH4, Acidic Hemorrhagic Metalloprotease from B. Aspervenom; Basp-I, Myotoxin I from B. Aspervenom; Basp-II, Myotoxin II from B. Aspervenom; and Basp-III, Myotoxin III from B. Aspervenom.” Biochemical Pharmacology, vol. 62, no. 11, Dec. 2001, pp. 1521–29. EBSCOhost, https://doi.org/10.1016/S0006-2952(01)00800-0.

APA

Trento, E. P., Garcia, O. S., Rucavado, A., França, S. C., Batalini, C., Arantes, E. C., Giglio, J. R., & Soares, A. M. (2001). Inhibitory properties of the anti-bothropic complex from Didelphis albiventrisserum on toxic and pharmacological actions of metalloproteases and myotoxins from bothrops asper venom11Abbreviations:SVMPs, snake venom metalloproteases; ABC, anti-bothropic complex from Didelphis albiventrisserum; DA43, 43-kDa subunit of anti-bothropic complex from D. albiventrisserum; DA45, 45-kDa subunit of anti-bothropic complex from D. albiventrisserum; MHD, dose able to induce a hemorrhagic lesion of 10 mm diameter; BaP1, basic hemorrhagic metalloprotease from Bothrops aspervenom; BaH4, acidic hemorrhagic metalloprotease from B. aspervenom; Basp-I, myotoxin I from B. aspervenom; Basp-II, myotoxin II from B. aspervenom; and Basp-III, myotoxin III from B. aspervenom. Biochemical Pharmacology, 62(11), 1521–1529. https://doi.org/10.1016/S0006-2952(01)00800-0

Chicago

Trento, Edilson P., Omar S. Garcia, Alexandra Rucavado, Suzelei C. França, Claudemir Batalini, Eliane C. Arantes, José R. Giglio, and Andreimar M. Soares. 2001. “Inhibitory Properties of the Anti-Bothropic Complex from Didelphis Albiventrisserum on Toxic and Pharmacological Actions of Metalloproteases and Myotoxins from Bothrops Asper Venom11Abbreviations:SVMPs, Snake Venom Metalloproteases; ABC, Anti-Bothropic Complex from Didelphis Albiventrisserum; DA43, 43-KDa Subunit of Anti-Bothropic Complex from D. Albiventrisserum; DA45, 45-KDa Subunit of Anti-Bothropic Complex from D. Albiventrisserum; MHD, Dose Able to Induce a Hemorrhagic Lesion of 10 Mm Diameter; BaP1, Basic Hemorrhagic Metalloprotease from Bothrops Aspervenom; BaH4, Acidic Hemorrhagic Metalloprotease from B. Aspervenom; Basp-I, Myotoxin I from B. Aspervenom; Basp-II, Myotoxin II from B. Aspervenom; and Basp-III, Myotoxin III from B. Aspervenom.” Biochemical Pharmacology 62 (11): 1521–29. doi:10.1016/S0006-2952(01)00800-0.