Abstract
When sections through rat neurohypophyses were treated with trypsin prior to incubation with enkephalin antibodies, vasopressin terminals invariably exhibited leucine-enkephalin-like immunoreactivity. Omitting tryptic cleavage the vasopressin terminals of some specimens only were immunostained. The enkephalin-like material was contained in the neurosecretory granules as shown by the protein A gold and the peroxidase anti-peroxidase method. We assume that the leucine-enkephalin sequence in vasopressin endings to some extent is present in a precursor form, possibly as dynorphin or α-neoendorphin, from which the pentapeptide is liberated by enzymatic cleavage.
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