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Substrate Specificity of Tissue Plasminogen Activator and Urokinase as Determined With Synthetic Chromogenic Substrates

Substrate Specificity of Tissue Plasminogen Activator and Urokinase as Determined With Synthetic Chromogenic Substrates

O Matsuo, T Sakai, Y Takakura, H Mihara

Jpn J Physiol. 1983;33(6):1031-7.

PMID: 6687071

Abstract:

Three different synthetic chromogenic substrates )H-glutamylglycyl-L-arginine-p-nitroanilide (S-2227), pyro-glutamyl-glycyl-L-arginine-p-nitroanilide (S-2444), and H-D-isoleucyl-L-prolyl-L-arginine-p-nitroanilide (S-2288] were investigated for use in the measurement of plasminogen activator activity with high molecular weight urokinase (H-UK), low molecular weight urokinase (L-UK), and tissue plasminogen activator (TPA). The three substrates were hydrolyzed by both TPA-type and UK-type plasminogen activator. As regards the amidolytic activity of S-2227, TPA exhibited a weaker amidolytic activity, and L-UK a stronger activity. In the case of the amidolytic activity of S-2444, no great difference between the three activators was observed in terms of Vmax. As regards the amidolytic activity of S-2288, L-UK exhibited a stronger activity, and TPA a weaker activity. It is suggested that the molecular size of the synthetic chromogenic substrate was too small when compared to natural substrate (fibrin), and therefore that fibrin-binding sites around the catalytic site in TPA are not recognized.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR4246520	Tissue plasminogen activator chromogenic substrate			Price

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