Abstract:
:Three unique inhibitors (SPAI-1, -+2, and -3) were first purified from porcine duodenal extract based on the Na+, K+-ATPase inhibitory activity. These peptide inhibitors had four disulfide bridges in common. The sequencing results of their S-carboxymethyl derivatives, lysilendopeptidase fragments, and chymotryptic peptides disclosed their entire primary structures. Both SPAI-2 and -3 consisted of 61 amino acids, respectively, and had almost the same sequences except for two amino acid substitutions, while SPAI-1 was found to lack the N-terminal twelve amino acid sequence of SPAI-2. The kinetics study revealed that SPAIs inhibited Na+, K+-ATPase by the competitive mode against Na+ and were uncompetitive with K+.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Araki K,Kuroki J,Ito O,Kuwada M,Tachibana Sdoi
10.1016/0006-291x(89)91747-6subject
Has Abstractpub_date
1989-10-16 00:00:00pages
496-502issue
1eissn
0006-291Xissn
1090-2104pii
0006-291X(89)91747-6journal_volume
164pub_type
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