Isolation of a New Phlorotannin, a Potent Inhibitor of Carbohydrate-Hydrolyzing Enzymes, from the Brown Alga Sargassum patens

2012 ◽  
Vol 60 (22) ◽  
pp. 5565-5570 ◽  
Author(s):  
Yasuko Kawamura-Konishi ◽  
Natsuko Watanabe ◽  
Miki Saito ◽  
Noriyuki Nakajima ◽  
Toshiyuki Sakaki ◽  
...  
2012 ◽  
Vol 104 ◽  
pp. 737-742 ◽  
Author(s):  
Demao Li ◽  
Limei Chen ◽  
Dong Xu ◽  
Xiaowen Zhang ◽  
Naihao Ye ◽  
...  

2012 ◽  
Vol 55 (6) ◽  
pp. 721-727 ◽  
Author(s):  
Joo Young Lee ◽  
Sang Min Kim ◽  
Woo-Suk Jung ◽  
Dae-Geun Song ◽  
Byung-Hun Um ◽  
...  

2006 ◽  
Vol 175 (4S) ◽  
pp. 255-256
Author(s):  
Cyrill A. Rentsch ◽  
Jeroen Buijs ◽  
Geertje Van der Horst ◽  
Petra Van Overveld ◽  
Antoinette Wetterwald ◽  
...  

Planta Medica ◽  
2009 ◽  
Vol 75 (09) ◽  
Author(s):  
AO Santos ◽  
EA Britta ◽  
T Ueda-Nakamura ◽  
BP Dias Filho ◽  
EM Bianco ◽  
...  

Planta Medica ◽  
2012 ◽  
Vol 78 (11) ◽  
Author(s):  
B Waltenberger ◽  
N Fakhrudin ◽  
M Cabaravdic ◽  
AG Atanasov ◽  
EH Heiss ◽  
...  
Keyword(s):  

1989 ◽  
Vol 61 (03) ◽  
pp. 437-441 ◽  
Author(s):  
Cindra Condra ◽  
Elka Nutt ◽  
Christopher J Petroski ◽  
Ellen Simpson ◽  
P A Friedman ◽  
...  

SummaryThe present work reports the discovery and charactenzation of an anticoagulant protein in the salivary gland of the giant bloodsucking leech, H. ghilianii, which is a specific and potent inhibitor of coagulation factor Xa. The inhibitor, purified to homogeneity, displayed subnanomolar inhibition of bovine factor Xa and had a molecular weight of approximately 15,000 as deduced by denaturing SDS-PAGE. The amino acid sequence of the first 43 residues of the H. ghilianii derived inhibitor displayed a striking homology to antistasin, the recently described subnanomolar inhibitor of factor Xa isolated from the Mexican leech, H. officinalis. Antisera prepared to antistasin cross-reacted with the H. ghilianii protein in Western Blot analysis. These data indicate that the giant Amazonian leech, H. ghilianii, and the smaller Mexican leech, H. officinalrs, have similar proteins which disrupt the normal hemostatic clotting mechanisms in their mammalian host’s blood.


1982 ◽  
Vol 47 (02) ◽  
pp. 173-176 ◽  
Author(s):  
E E Nishizawa ◽  
A R Mendoza ◽  
T Honohan ◽  
K A Annis

SummaryA thiazole derivative, 4,5-bis(p-methoxyphenyl)-2-(trifluoromethyl)-thiazole was found to be a potent inhibitor of collagen-induced platelet aggregation, in vitro, using platelets from at least six species, including man. It was active in human platelet-rich plasma at a concentration of 1 ng/ml. While its antiplatelet activity was greater than that of flurbiprofen, its cyclooxygenase activity was equivalent to that of flurbiprofen. Also, compared to flurbiprofen, the thiazole had less anti-inflammatory activity in the hind-paw edema test. The thiazole derivative inhibited platelet aggregation following oral administration in five laboratory species. In the guinea pig it was active at 0.5 mg/kg. The LD50 in mice was greater than 1000 mg/kg (i.p.). This compound, which was designed through a systematic drug development program, may have high potential as an antithrombotic agent.


Sign in / Sign up

Export Citation Format

Share Document