MONOCLONAL-ANTIBODIES ALLOW PRECIPITATION OF ESTERASIC BUT NOT PEPTIDASIC ACTIVITIES ASSOCIATED WITH BUTYRYLCHOLINESTERASE
MONOCLONAL-ANTIBODIES ALLOW PRECIPITATION OF ESTERASIC BUT NOT PEPTIDASIC ACTIVITIES ASSOCIATED WITH BUTYRYLCHOLINESTERASE
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DOI：
10.1111/j.1471-4159.1990.tb04555.x
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发表时间：
1990-09-01
影响因子：
4.7
通讯作者：
VINCENT, JP
中科院分区：
文献类型：
--
作者：
CHECLER, F;GRASSI, J;VINCENT, JP
Commercially available and affinity-purified butyrylcholinesterases isolated from human serum were examined for their esterasic activity and their ability to hydrolyze various neuropeptides, including neurotensin, substance P, and leucine-enkaphalin. The three pools that displayed the lowest esterasic activities were shown to hydrolyze neurotensin with the same HPLC degradative pattern. By contrast, noticeable qualitative and quantitative discrepancies were observed when hydrolyses of substance P and leucine-enkephalin by these three butyrylcholinesterase pools were studied. The pool that exhibited the highest esterasic activity appeared to be homogeneously constituted by 90- and 180-kDa protein bands by sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis and was totally unable to hydrolyze these three neuropeptides. This suggested that the three other butyrylcholinerase preparations could be contaminated by exogenous peptidases. This was confirmed by means of three distinct monoclonal antibodies directed toward human serum butyrylcholinesterase. The three IgG-purified fractions precipitated the esterasic activity, whereas they failed to precipitate the neuropeptidase-hydrolyzing activities whatever the substrate examined. Altogether, these results demonstrate that peptidases associated with butyrylcholinesterase are contaminating enzymes that cannot be considered as intrinsic activities of this enzyme.
