h-phe-gln-val-val-cys(npys)-gly-nh2

[ 密度 ]:
1.38g/cm3

[ 沸点 ]:
1152.3ºC at 760mmHg

[ 分子式 ]:
C₃₄H₄₈N₁₀O₉S

[ 分子量 ]:
772.87200

[ 闪点 ]:
650.7ºC

[ 精确质量 ]:
772.33300

[ PSA ]:
341.71000

[ LogP ]:
3.34870

[ 蒸汽压 ]:
0mmHg at 25°C

[ 折射率 ]:
1.63

[ 个人防护装备 ]:
Eyeshields;Gloves;type N95 (US);type P1 (EN143) respirator filter

[ 危险品运输编码 ]:
NONH for all modes of transport

Design and synthesis of a kininogen-based selective inhibitor of thrombin-induced platelet aggregation.

Pept. Res. 7 , 32-35, (1994)

Thrombin-induced platelet aggregation has been suggested to play an important role in reocclusion following thrombolytic therapy or angioplasty for treatment of myocardial infarction. We previously de...

Modulation of thrombin-induced platelet aggregation by inhibition of calpain by a synthetic peptide derived from the thiol-protease inhibitory sequence of kininogens and S-(3-nitro-2-pyridinesulfenyl)-cysteine.

Eur. J. Biochem. 214 , 233-241, (1993)

Thrombin-induced platelet aggregation has been suggested to play an important role in reocclusion following thrombolytic therapy of angioplasty for treatment of myocardial infarction. We previously de...

Specificity of the sequence in Phe-Gln-Val-Val-Cys (-3-nitro-2-pyridinesulfenyl)-Gly-NH2--a selective inhibitor of thrombin-induced platelet aggregation.

Thromb. Res. 72 , 183, (1993)

Thrombin-induced platelet aggregation is mediated in part by the intracellularly activated calpain expressed onto the external side of the membrane. We have previously shown that P1, Phe-Gln-Val-Val-C...

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