Inhibition of inflammatory proteinase, medullasin, by alpha 2-macroglobulin and ovomacroglobulin.
The in vitro activity of inflammatory proteinase, medullasin, was stoichiometrically inhibited by a serum proteinase inhibitor, alpha 2-macroglobulin, and its homolog, chicken ovomacroglobulin. The two inhibitors were cleaved by medullasin only in the bait region. The effectiveness of alpha 2-macroglobulin to inhibit medullasin in competition with alpha -1-proteinase inhibitor was measured under a simulated in vivo condition and an estimation was made that about 60-70% medullasin is inhibited by alpha-1-inhibitor and 30-40% by alpha 2-macroglobulin.
Ikai
A
A
Dept. of Biophysics and Biochemistry, Faculty of Science, Univ. of Tokyo, Japan.
Nakashima
M
M
Aoki
Y
Y
D001667:Binding, Competitive; D001798:Blood Proteins / Q000494:pharmacology; D001853:Bone Marrow / Q000201:enzymology*; D002918:Chymotrypsin / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008259:Macroglobulins / Q000494:pharmacology*; D008970:Molecular Weight; D011480:Protease Inhibitors; D012697:Serine Endopeptidases / Q000378:metabolism; D015842:Serine Proteinase Inhibitors; D014357:Trypsin / Q000378:metabolism; D000515:alpha 1-Antitrypsin; D000511:alpha-Macroglobulins / Q000494:pharmacology*
D001798:Blood Proteins; D008259:Macroglobulins; D011480:Protease Inhibitors; D015842:Serine Proteinase Inhibitors; D000515:alpha 1-Antitrypsin; D000511:alpha-Macroglobulins; C036828:ovomacroglobulin; D012697:Serine Endopeptidases; C034869:medullasin; D002918:Chymotrypsin; D014357:Trypsin