作者: T.W. Schwartz
DOI: 10.1016/S0021-9258(18)61158-5
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摘要: Abstract The processing of the common precursor for pancreatic polypeptide and icosapeptide was studied in primary cultures endocrine cells isolated from duodenal part canine pancreas. Biosynthetically labeled peptides were characterized by enzymatic digestion radiosequencing compared to a COOH-terminally extended form which pancreas also sequenced. It substantiated that, these cell cultures, can be at classical dibasic site between icosapeptide, monobasic its COOH-terminal extension. Pulse-chase experiments showed that cleavage occurs later than one biosynthetic process; apparently not cleaved before prohormone had been processed site. could distinguished mechanism as, time, gradually lost ability cleave while unaffected. is concluded conversion, important activation series hormones, neuropeptides, growth factors, distinct cellular mechanism.