@Article{biocell.2007.31.355,
AUTHOR = {S.L. MARUÑAK, L. LEIVA, M.E. GARCIA DENEGRI, P. TEIBLER, O. ACOSTA DE PÉREZ},
TITLE = {Isolation and biological characterization of a basic phospholipase A<sub>2</sub> from <i>Bothrops jararacussu</i> snake venom},
JOURNAL = {BIOCELL},
VOLUME = {31},
YEAR = {2007},
NUMBER = {3},
PAGES = {355--364},
URL = {http://www.techscience.com/biocell/v31n3/33926},
ISSN = {1667-5746},
ABSTRACT = {A phospholipase A<sub>2</sub>
 has been isolated from <i>Bothrops jararacussu</i> venom from snakes that
inhabit the northeast region of Argentina. The present study describes <i>in vivo</i> and <i>in vitro</i> biological activities
of phospholipase A<sub>2</sub>
 from <i>B. jararacussu</i> as well as isolation details of its. Venom was obtained by milking of
adult snakes which were housing in wood reptile cages of varying dimensions in heated (20–30ºC) rooms.
Snakes received a weekly diet of mice and water was available ad libitum for drinking and soaking. The
enzyme was purified by gel filtration on a Sephadex G-75 column followed by ion exchange chromatography
on a SP-Sephadex C25 column. The major peak belonging to proteins was retained in the cation exchanger
and then eluted using a concentration gradient of KCl that exhibited phospholipase activity.<br/>

This basic PLA<sub>2</sub>
 consists of a single polypeptide chain with a molecular mass of 15.6 kDa. It had a high
indirect hemolytic activity and produced a significant paw edema reaction in mice. The enzyme showed a low
lethality (LD<sub>50</sub> 148.6 µg) when was administered i.p. but exhibited elevated myotoxic effects <i>in vivo</i> by
increasing plasma CK activity of injected mice, corroborated results by the histological observations of samples
of gastrocnemius muscle. Myonecrosis is the result of intense destruction of muscular fibers that involves
local infiltration of inflammatory cells and leads to the highest peak of CK level just after 1 hour mice
injection. Moreover, the isolated enzyme showed anticoagulant activity, evaluated on sheep platelet-poor
plasma which recalcification time was prolonged after incubation with the isolated phospholipase A<sub>2</sub>
. These
findings showed that this phospholipase, isolated by only two simple chromatographic steps, possesses high
edematogenic and myotoxic activities. However, despite the low lethal activity, this enzyme would contribute
markedly to the pathophysiology of the bothropic envenomation.},
DOI = {10.32604/biocell.2007.31.355}
}