Inhibition by leupeptin and antipain of the intracellular proteolysis of Ii
QV Nguyen, W Knapp, RE Humphreys - Human immunology, 1989 - Elsevier
Intracellular cleavage of I i was evaluated in immunoprecipitates of radiolabeled Raji cells
treated with protease inhibitors (leupeptin, antipain, chymostatin, and pepstatin) or blockers
of endosomal function (chloroquine and monensin). Immunoprecipitates with anti-class II
and anti-I i (12–28) sera and VIC-Y1 MoAb revealed I i cleavage products of 21,000 and
10,000 daltons (p21 and p10) only in leupeptin-and antipain-treated cells. Both p21 and p10
were judged to be N-terminal products because they were recognized with anti-I i (12–28) …
treated with protease inhibitors (leupeptin, antipain, chymostatin, and pepstatin) or blockers
of endosomal function (chloroquine and monensin). Immunoprecipitates with anti-class II
and anti-I i (12–28) sera and VIC-Y1 MoAb revealed I i cleavage products of 21,000 and
10,000 daltons (p21 and p10) only in leupeptin-and antipain-treated cells. Both p21 and p10
were judged to be N-terminal products because they were recognized with anti-I i (12–28) …