Abstract
The amino acid sequence of radioimmunoassayable neurotensin, isolated from bovine small intestinal extracts, has been shown to be the same as that of the peptide originally isolated from bovine hypothalamic extracts. This was accomplished by sequence studies on the intact peptide as well as on its chymotryptic and papain-generated fragments. Thus, neurotensin joins the group of biologically active peptides shown to be present in the same molecular form in both brain and intestine.
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