[Inhibition of human granulocyte elastase by antibodies to leukocyte thermostable alpha-glycoprotein].
The activity of granulocyte elastase (GE) was discovered in the preparations of leukocyte thermostable alpha-glycoprotein (LTG) isolated from pus by means of ion-exchange chromatography. The activity of GE was determined according to MeoSuc(Ala)2ProValpNa hydrolysis. The antibodies against LTG were isolated from monospecific antisera. Sepharose with immobilized fraction of pus proteins was utilized as immunosorbent. Isolated antibodies to LTG inhibited the GE activity. An inhibitory effect of antibodies increased with the increase in their concentration. The identity or binding of LTG and GE was suggested. The binding of LTG with pus protein component was discovered, the biological meaning of this phenomenon being unknown.
Shevchenko
O P
OP
Eremenko
O V
OV
Ogloblina
O G
OG
Sorochinskaia
E I
EI
D000906:Antibodies / Q000276:immunology*; D001798:Blood Proteins / Q000276:immunology*; D006023:Glycoproteins / Q000097:blood / Q000276:immunology*; D006098:Granulocytes / Q000201:enzymology*; D006801:Humans; D011480:Protease Inhibitors / Q000097:blood*
D000906:Antibodies; D001798:Blood Proteins; D006023:Glycoproteins; D011480:Protease Inhibitors
Ingibirovanie élastazy granulotsitov cheloveka antitelami protiv leĭkotsitarnogo termostabil'nogo al'fa-glikoproteida.