TY - JOUR
T1 - Protein isolation and identification of Pterois volitans spine venom coagulant activity
AU - Sommeng, A. N.
AU - Eka, A. K.
AU - Ramadhan, M. Y.A.
AU - Ginting, M. J.
AU - Sahlan, M.
AU - Hermansyah, H.
AU - Wijanarko, A.
N1 - Publisher Copyright:
© Published under licence by IOP Publishing Ltd.
PY - 2020/4/15
Y1 - 2020/4/15
N2 - Pterois volitans, or commonly referred to lionfish, are fish species originating from Indo-Pacific waters but are becoming invasive in other regions such as the Caribbean and Atlantis. Various efforts have been made to reduce the number of lionfish, and one of them is by utilizing the venom on the spine. The venom extraction of P. volitans spines is done mechanically using sonication and centrifugation, and then protein isolation is carried out using salt. Coagulant activity from extract (crude venom) and lionfish venom protein isolate was done by counting PT (prothrombin time) and aPTT (activated partial thromboplastin time) which resulted that the crude venom and protein isolate of lionfish venom can accelerate blood clot (procoagulant) respectively up to 8.5 seconds and 6 seconds. Protein identification was made using LC-MS/MS device. The LC-MS/MS analysis showed that the protein isolate of lionfish venom contains Nomega-nitro-L-arginine methyl ester (L-NAME) compounds known to have procoagulant effects. From a series of tests mentioned, it concluded that P. volitans venom have procoagulant activity and one of the compounds responsible for it is L-NAME.
AB - Pterois volitans, or commonly referred to lionfish, are fish species originating from Indo-Pacific waters but are becoming invasive in other regions such as the Caribbean and Atlantis. Various efforts have been made to reduce the number of lionfish, and one of them is by utilizing the venom on the spine. The venom extraction of P. volitans spines is done mechanically using sonication and centrifugation, and then protein isolation is carried out using salt. Coagulant activity from extract (crude venom) and lionfish venom protein isolate was done by counting PT (prothrombin time) and aPTT (activated partial thromboplastin time) which resulted that the crude venom and protein isolate of lionfish venom can accelerate blood clot (procoagulant) respectively up to 8.5 seconds and 6 seconds. Protein identification was made using LC-MS/MS device. The LC-MS/MS analysis showed that the protein isolate of lionfish venom contains Nomega-nitro-L-arginine methyl ester (L-NAME) compounds known to have procoagulant effects. From a series of tests mentioned, it concluded that P. volitans venom have procoagulant activity and one of the compounds responsible for it is L-NAME.
UR - http://www.scopus.com/inward/record.url?scp=85085014588&partnerID=8YFLogxK
U2 - 10.1088/1755-1315/462/1/012039
DO - 10.1088/1755-1315/462/1/012039
M3 - Conference article
AN - SCOPUS:85085014588
SN - 1755-1307
VL - 462
JO - IOP Conference Series: Earth and Environmental Science
JF - IOP Conference Series: Earth and Environmental Science
IS - 1
M1 - 012039
T2 - 3rd International Conference on Natural Products and Bioresource Sciences 2019, ICONPROBIOS 2019
Y2 - 23 October 2019 through 24 October 2019
ER -