Abstract：
:Chromatography on a column of SP-Sephadex shows that commercial chymopapain contains three components with proteolytic activity. Each behaves as a single protein upon rechromatography and electrophoresis on polyacrylamide gels. The major component, which represents 31% of the activity applied to the column and is the most basic protein, was identified as papaya peptidase A. This enzyme has no methionine and isoleucine on its N-terminus. Its molecular weight is about 24,000 as determined by sodium dodecyl sulfate polyacrylamide electrophoresis and sedimentation equilibrium centrifugation. Its fluorescence emission as a function of pH resembles that for unactivated papain. Reduction is required for full activity, and in general it is less active than papain against substrates such as casein, N-benzoyl-L-arginine ethyl ester, N-tosyl-L-arginine methyl ester, N-benzoyl-L-arginineamide, and N-benzoyl-DL-arginine p-nitroanilide. Of the other components isolated from crude chymopapain, the more acidic enzyme contains 20% of the activity applied to the column, has a molecular weight of about 25,000, and N-terminal residues of tyrosine and glutamic acid. The other enzyme represents 26% of the initial activity, has a molecular weight of about 28,000 and tyrosine on its N-terminus. Both proteins have a single residue of methionine per molecule. The more acidic component resembles chymopapain A, and the other enzyme is similar to chymopapain B.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Robinson GWdoi
10.1021/bi00687a028subject
Has Abstractpub_date
1975-08-12 00:00:00pages
3695-700issue
16eissn
0006-2960issn
1520-4995journal_volume
14pub_type
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