Abstract：
:The exopeptidases dipeptidyl aminopeptidases I and IV were used to hydrolyze the N-terminal portion of spinach plastocyanin to dipeptides. The enzymes were used individually as well as in a mixture and the dipeptides were analyzed by combined gas chromatography-mass spectrometry. Data are presented for native plastocyanin and the S-methylated protein. Of the 98 residues which make up this protein, the first 44 were released in the form of 22 dipeptides by the combined action of DAP I and DAP IV. These dipeptides were aligned by homology to other plastocyanins of known sequence. The results demonstrate the versatility of the two enzymes in hydrolyzing proteins to obtain information on their primary sequence.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Seifert WE Jr,Caprioli RMdoi
10.1021/bi00596a009subject
Has Abstractpub_date
1978-02-07 00:00:00pages
436-41issue
3eissn
0006-2960issn
1520-4995journal_volume
17pub_type
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