[Antiproteinase activity of alpha 2-macroglobulin].
Blood serum separation by the method of gel filtration on Sephadex G-200 with the subsequent immunochemical determination of the quantitative content of basic proteolysis inhibitors permitted isolating the alpha 2-macroglobulin fraction while alpha 1-antitrypsin and alpha 1-antichymotrypsin separation was a failure. The immunochemical analysis of the antienzymic activity of the isolated inhibitors showed that 32.3 +/- 3.5% of the introduced kallikrein, 18.7 +/- 0.6% of trypsin and 14.4 +/- 4.1% of chymotrypsin were bound in the zone of alpha 2-macroglobulin. The rest of antienzymic activity was localized in the zone of alpha 1-antitrypsin and alpha 1-antichymotrypsin. After a preliminary saturation of blood serum with trypsin in the amount equivalent to its antitryptic capacity (200 micrograms/ml) the ability of alpha 2-macroglobulin to bind kallikrein and chymotrypsin lowers considerably (by 69 and 72%, respectively). In the zone of alpha 1-antitrypsin and alpha 1-antichymotrypsin a decrease in the ability to bind kallikrein and chymotrypsin amounted to 44 and 12% respectively. Thus, alpha 2-macroglobulin being bound with trypsin looses considerably its ability to bind other enzymes.
D002850:Chromatography, Gel; D002918:Chymotrypsin / Q000037:antagonists & inhibitors / Q000097:blood; D006801:Humans; D011480:Protease Inhibitors / Q000097:blood*; D014361:Trypsin Inhibitors / Q000097:blood; D000511:alpha-Macroglobulins / Q000032:analysis*
D011480:Protease Inhibitors; D014361:Trypsin Inhibitors; D000511:alpha-Macroglobulins; D002918:Chymotrypsin
Antiproteinaznaia aktivnost' alpha 2-makroglobulina.