| Autor: |
Andreasen, P.A., Riccio, A., Welinder, K.G., Douglas, R., Sartorio, R., Nielsen, L.S., Oppenheimer, C., Blasi, F., Danø, K. |
| Zdroj: |
FEBS Letters; January 1986, Vol. 209 Issue: 2 p213-218, 6p |
| Abstrakt: |
Both the urokinase-type and tissue-type plasminogen activator can convert their 5̃4 kDa type-1 inhibitor (PAI-1) to an inactive form with a lower apparent molecular mass. We have determined the amino-terminal amino acid sequences of human native and converted PAI-1, and isolated PAI-1 cDNA and determined the nucleotide sequence in regions corresponding to the amino-terminus and the cleavage site. The data show that the conversion of the inhibitor consists of cleavage of an Arg-Met bond 33 residues from the carboxy-terminus, thus localizing the reactive center of the inhibitor to that position. In addition, a heterogeneity was found at the amino-terminus, with a Ser-Ala-Val-His-His form and a two-residue shorter form (Val-His-His-) occurring in approximately equal quantities. |
| Databáze: |
Supplemental Index |
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