| Autor: |
Gerencer M; Tissue typing Centre, Department of Cellular Immunology, University Hospital KBC, HR-10000 Zagreb, Kispaticeva 12, Croatia. gerencm@baxter.com, Burek V |
| Jazyk: |
angličtina |
| Zdroj: |
Virus research [Virus Res] 2004 Sep 15; Vol. 105 (1), pp. 97-100. |
| DOI: |
10.1016/j.virusres.2004.04.010 |
| Abstrakt: |
We have investigated the ability of HIV-1 protease to cleave human complement proteins of the classical complement pathway: C1q, C2 and C4 as well as the regulatory protein, C1-inhibitor. Purified complement proteins were incubated with recombinant HIV-1 protease in vitro and analyzed by SDS-PAGE and immunoblotting assay. The only cleavage site was found in N-terminal region of C1-inhibitor, and it was located between residues Leu-32 and Phe-33 as determined by amino acid sequence analysis of the 85 kDa proteolytic fragment after 12 Edman degradation cycles. The HIV-1 protease cleavage sites were not found in C1q, C2 and C4 protein. HIV-1 protease-susceptible site in N-terminal region of C1-inhibitor is very close to the cleavage sites of some other proteases that are able to induce N-terminal proteolysis of the protein. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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