Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.23.16 (HIV-1 protease)
2,107 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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.
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PMID:Identification of HIV-1 protease cleavage site in human C1-inhibitor. 1532 85