THE IN-VITRO INHIBITION OF PROTEASES FROM CRYPTOBIA-SALMOSITICA KATZ BY A MONOCLONAL-ANTIBODY (MAB-001) AGAINST A GLYCOPROTEIN ON THE PATHOGENIC HEMOFLAGELLATE
X. Zuo et al., THE IN-VITRO INHIBITION OF PROTEASES FROM CRYPTOBIA-SALMOSITICA KATZ BY A MONOCLONAL-ANTIBODY (MAB-001) AGAINST A GLYCOPROTEIN ON THE PATHOGENIC HEMOFLAGELLATE, Journal of fish diseases, 20(6), 1997, pp. 419-426
The monoclonal antibody (MAb-001), which was produced against a surfac
e membrane glycoprotein on C. salmositica, significantly inhibited the
activities of the intracellular proteases of the parasite. The total
activity in the partially purified metallo-protease, and about 80% of
activity in the partially purified cysteine protease, were inhibited b
y the antibody (at 10 mu g protein ml(-1)). The inhibitory effects of
the antibody on the proteases were also demonstrated using haemoglobin
(substrate)-SDS-PAGE. The activities of the metallo-protease band (20
0 kDa) and the three cysteine protease bands (66, 70 and 97 kDa) were
inhibited by MAb-001, but the activity of the fourth cysteine protease
band (49 kDa) was not affected. Similar inhibitory effects of the ant
ibody were also found in the crude protease extract (parasite lysate),
except that more antibody was required to obtain the same level of in
hibition. The metallo-protease band was more sensitive than the cystei
ne protease bands to the antibody.