Acacia Proteinase Inhibitors

Biochemical characterization of Acacia schweinfurthii serine proteinase inhibitor.

One of the many control mechanisms of serine proteinases is their specific inhibition by protein proteinase inhibitors. An extract of Acacia schweinfurthii was screened for potential serine proteinase inhibition. It was successfully purified to homogeneity by precipitating with 80% (v/v) acetone and sequential chromatographic steps, including ion-exchange, affinity purification and reversed-pha...

Proteinase inhibitors in rheumatoid arthritis.

The concentrations of five normally occurring protease inhibitors in serum and synovial fluid were compared in patients with rheumatoid arthritis, osteoarthrosis, and normal controls. The patients with rheumatoid arthritis showed a significant rise in alpha1-antitrypsin, alpha1-antichymotrypsin, and inter-alpha-trypsin inhibitor (in decreasing order) in serum as well as in synovial fluid. In sy...

Proteinase inhibitors in rat serum

Three different serine proteinase inhibitors were isolated from rat serum and purified to apparent homogeneity. One of the inhibitors appears to be homologous to a1-proteinase inhibitor isolated from man and other species, but the other two, designated rat proteinase inhibitor I and rat proteinase inhibitor II, seem to have no human counterpart. ac-Proteinase inhibitor (Mr 55000) inhibits tryps...

Mechanism-based proteinase inhibitors: a critical review.

The efficacy of a mechanism-based enzyme inhibitor depends not only on the rate of covalent modification of the target enzyme, but also on the affinity with which the enzyme binds the inhibitor before covalent bond formation. Since proteinases have binding regions that extend many residues beyond the scissile peptide bond, specific and potent mechanism-based inhibitors of this class of enzyme c...

PROTEINASE INHIBITORS Medical and Biological Aspects