Synthesis and structural analysis of curdlan sulfate with a potent inhibitory effect in vitro of AIDS virus infection

1990 ◽  
Vol 23 (16) ◽  
pp. 3717-3722 ◽  
Author(s):  
Takashi Yoshida ◽  
Kenichi Hatanaka ◽  
Toshiyuki Uryu ◽  
Yutaro Kaneko ◽  
Eiichiro Suzuki ◽  
...  
1994 ◽  
Vol 27 (22) ◽  
pp. 6272-6276 ◽  
Author(s):  
Takashi Yoshida ◽  
Yuichi Yasuda ◽  
Toshiyuki Uryu ◽  
Hideki Nakashima ◽  
Naoki Yamamoto ◽  
...  

1979 ◽  
Author(s):  
J. Hawiger ◽  
S. Parkinson ◽  
S. Timmons

Fibrinogen is a plasma factor required for aggregation of human platelets by ADP. The mechanism of platelet-ADP-fibrinogen interaction was studied by measuring the equilibrium binding of 125I-fibrinogen to human platelets separated from plasma proteins. Binding of 125I-fibrinogen to platelets not stimulated with ADP was low and unaffected by an excess of unlabel led fibrinogen. However, when platelets were stimulated with 4μM of ADP, there was an eightfold increase In the number of available binding sites for human fibrinogen, with affinity constant of 1.9 x 109M-1. This striking increase in fibrinogen receptor sites on human platelets was specific for ADP as contrasted to ATP, AMP, and adenosine. Prostacyclin (Prostaglandin I2, PGI2), a novel prostaglandin produced by the blood vessel wall, completely blocked this ADP-induced increase in fibrinogen receptor sites on human platelets. The effect of PGI2 was prompt and concentration dependent, reaching maximum at 10-9M. 6-keto PGF2 a stable derivative ot PGI2, did not have such an effect. Thus movement of fibrinogen receptor sites on human platelet membrane stimulated with ADP is prevented by PGI2. This represents a new biologic property of this vascular hormone and contributes to better understanding of its potent inhibitory effect in vitro and in vivo on ADP-induced platelet aggregation requiring mobilization of fibrinogen receptor.


Nature ◽  
1969 ◽  
Vol 223 (5208) ◽  
pp. 845-846 ◽  
Author(s):  
PADMAN S. SARMA ◽  
GRACE SHIU ◽  
SAMUEL BARON ◽  
R. J. HUEBNER

Nature ◽  
1969 ◽  
Vol 224 (5219) ◽  
pp. 604-605 ◽  
Author(s):  
PADMAN S. SARMA ◽  
SAMUEL BARON ◽  
ROBERT J. HUEBNER ◽  
GRACE SHIU

1998 ◽  
Vol 30 (3) ◽  
pp. 243-248 ◽  
Author(s):  
Ying Gao ◽  
Kaname Katsuraya ◽  
Yutaro Kaneko ◽  
Toru Mimura ◽  
Hideki Nakashima ◽  
...  

2003 ◽  
Vol 65 (1) ◽  
pp. 35-42 ◽  
Author(s):  
Alice Wattel ◽  
Said Kamel ◽  
Romuald Mentaverri ◽  
Florence Lorget ◽  
Christophe Prouillet ◽  
...  

2016 ◽  
Vol 06 (01) ◽  
pp. 9-16 ◽  
Author(s):  
Asad M. Ilyas ◽  
Youssri Ahmed ◽  
Mamdooh Gari ◽  
Mohammed H. Alqahtani ◽  
Taha A. Kumosani ◽  
...  

2021 ◽  
Vol 8 ◽  
Author(s):  
Jiayue Guo ◽  
Alyssa Gutierrez ◽  
Libo Tan ◽  
Lingyan Kong

Ascorbic acid, also known as vitamin C, was previously reported to inhibit the activity of pancreatic α-amylase, the primary digestive enzyme for starch. A major implication of such inhibition is a slowed rate of starch digestion into glucose, which thereby reduces postprandial hyperglycemia. The aim of this study was to explore the inhibitory effects of ascorbic acid at various concentrations on the in vitro digestion of high amylose maize starch (HAMS) and potato starch (PS) in both raw and cooked conditions. Resistant starch (RS) content, defined as the starch that remained after 4 h of simulated in vitro enzymatic digestion, was measured for the starch samples. Upon the addition of ascorbic acid, the RS contents increased in both raw and cooked starches. Cooking significantly reduced the RS contents as compared to raw starches, and less increase in RS was observed with the addition of ascorbic acid. The inhibitory effect of ascorbic acid on the digestion of raw starches showed a dose-dependent trend until it reached the maximum extent of inhibition. At the concentrations of 12.5 and 18.75 mg/mL, ascorbic acid exhibited the most potent inhibitory effect on the in vitro starch digestion in raw and cooked conditions, respectively. Overall, our results strongly indicate that ascorbic acid may function as a glycemic modulatory agent beyond other important functions, and its effects persist upon cooking with certain concentrations applied.


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