title: Leucine-enkephalin-like immunoreactivity in vasopressin terminals is enhanced by treatment with peptidases.
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 alpha-neo-endorphin, from which the pentapeptide is liberated by enzymatic cleavage.
mesh_terms: D000818:Animals; D004743:Enkephalin, Leucine / Q000276:immunology*; D009411:Nerve Endings / Q000276:immunology*; D009490:Neurosecretory Systems / Q000276:immunology; D051381:Rats; D011910:Rats, Brattleboro; D014357:Trypsin / Q000494:pharmacology*; D014667:Vasopressins / Q000502:physiology*
chemical_list: D014667:Vasopressins; D004743:Enkephalin, Leucine; D014357:Trypsin