InChI
1S/C8H6Br2O/c9-5-8(11)6-1-3-7(10)4-2-6/h1-4H,5H2
InChI key
FKJSFKCZZIXQIP-UHFFFAOYSA-N
SMILES string
BrCC(=O)c1ccc(Br)cc1
assay
≥98% (HPLC)
form
powder
color
yellow to brown
mp
108-110 °C (lit.)
storage temp.
2-8°C
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Rodrigo G Stábeli et al.
Comparative biochemistry and physiology. Toxicology & pharmacology : CBP, 142(3-4), 371-381 (2006-01-31)
MjTX-II, a myotoxic phospholipase A(2) (PLA(2)) homologue from Bothrops moojeni venom, was functionally and structurally characterized. The MjTX-II characterization included: (i) functional characterization (antitumoral, antimicrobial and antiparasitic effects); (ii) effects of structural modifications by 4-bromophenacyl bromide (BPB), cyanogen bromide (CNBr)
Youngjin Park et al.
Archives of insect biochemistry and physiology, 60(3), 105-115 (2005-10-20)
We report on a secretory phospholipase A2 (sPLA2) associated with membrane-enriched fractions prepared from hemocytes of the tobacco hornworms, Manduca sexta. Virtually no PLA2 activity was detected in serum of immunologically naive or bacterially challenged hornworms. PLA2 activity was detected
Daniela P Marchi-Salvador et al.
Biochimica et biophysica acta, 1794(11), 1583-1590 (2009-07-21)
For the first time, the structure of a catalytic inactive phospholipase A(2) homolog (Lys49-PLA(2)s) complexed with p-bromophenacyl bromide (BPB) has been solved by X-ray crystallography. Lys49-PLA(2)s are among the main components of Viperidae snake venoms, causing myonecrosis and other actions
Wen-Hsin Liu et al.
Toxicology letters, 185(2), 102-109 (2009-01-03)
In view of the controversial role of catalytic activity on the cytotoxicity of phospholipase A(2) (PLA(2)), the present study is conducted to explore whether PLA(2) induces apoptotic process of human leukemia U937 cells through catalytic activity-independent pathway. Modification of His-48
Angelo J Magro et al.
Acta crystallographica. Section D, Biological crystallography, 61(Pt 12), 1670-1677 (2005-11-23)
The crystal structure of an acidic phospholipase A(2) isolated from Bothrops jararacussu venom (BthA-I) chemically modified with p-bromophenacyl bromide (BPB) has been determined at 1.85 Angstroms resolution. The catalytic, platelet-aggregation inhibition, anticoagulant and hypotensive activities of BthA-I are abolished by
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