Elucidation of cathepsin B-like activity associated with extracts of human myelin basic protein.
Myelin basic protein (MBP) extracted from human delipidated white matter was found to be degraded at pH 3.0 by endogenous proteolytic activities of extracts. Electrophoretic peptide patterns were consistent with limited proteolysis of MBP. Based on pH, activation by EDTA and DTE, and inhibition by p-CMPS, E-64 and, in particular, by leupeptin, the protease involved was tentatively identified as cathepsin B or a cathepsin B-like enzyme. As pepstatin failed to inhibit acid proteolysis of MBP cathepsin D was ruled out.
Berlet
H H
HH
Ilzenhöfer
H
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D002731:4-Chloromercuribenzenesulfonate / Q000494:pharmacology; D002401:Cathepsin B; D002403:Cathepsins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D004226:Dithioerythritol / Q000494:pharmacology; D004492:Edetic Acid / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007930:Leucine / Q000031:analogs & derivatives / Q000494:pharmacology; D007976:Leupeptins / Q000494:pharmacology; D004676:Myelin Basic Protein / Q000378:metabolism*; D011480:Protease Inhibitors / Q000494:pharmacology
D007976:Leupeptins; D004676:Myelin Basic Protein; D011480:Protease Inhibitors; D002731:4-Chloromercuribenzenesulfonate; D004226:Dithioerythritol; D004492:Edetic Acid; D002403:Cathepsins; D002401:Cathepsin B; D007930:Leucine; C032854:leupeptin; C024974:E 64