Structure of Porcine Cholecystokinin‐Pancreozymin
作者： V. Mutt , J. E. Jorpes
DOI: 10.1111/J.1432-1033.1968.TB00433.X
关键词: Methionine 、 Peptide 、 Peptide bond 、 Cholecystokinin 、 Tyrosine 、 Trypsin 、 Chemistry 、 Stereochemistry 、 Amino acid 、 Threonine
摘要: Cholecystokinin-pancreozymin has been found to have the partial structure Lys (Ala1, Gly1, Pro1, Ser1) · Arg Val (Ile1, Met1, Asn (Asx1, Glx1, His1, Leu2, Ser2) Arg. Ile (Asp1, Asp [Gly1, Met2, Trp1, Tyr (SO3H)] Phe NH2. Of four peptide bonds in this polypeptide, three arginyl and one lysyl, that are cleaved by trypsin only arginyl-valine bond is thrombin, with retention of cholecystokinin pancreozymin activities original molecule C-terminal heptacosapeptide. The tryptic octapeptide too strong activity. Except for replacement a threonine methionine eight amino acid units same as those comprise corresponding part caerulein. Also like caerulein, phenolic group tyrosine cholecystokinin-pancreozymin esterified sulphuric acid.
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