Proteolysis of adrenocorticotropin in brain. Characterization of cleavage sites by peptidases in synaptic membranes and formation of peptide fragments.
作者： X C Wang , J P Burbach , C J Verhoef , D De Wied
DOI: 10.1016/S0021-9258(20)82009-2
关键词:
摘要: The biotransformation of adrenocorticotropin (ACTH-(1-39)) by brain synaptic membranes has been studied. Peptide fragments ACTH-(1-39) which were formed during in vitro incubation the peptide with membrane preparations isolated high pressure liquid chromatography and characterized determination amino acid composition NH2- terminal residue. At pH 7.4, ACTH-(1-38) was found as main metabolite, together ACTH-(7-21) ACTH-(7-20). In addition, a series secondary products identified. 6.2, ACTH-(1-38), ACTH-(1-37), ACTH-(1-36) exclusively formed, while at 8.5, converted into ACTH-(1-16), ACTH-(17-39), ACTH-(22-39), ACTH-(3-15). Time course experiments demonstrated action carboxypeptidase activity trypsin-like endopeptidase on predominant proteolytic events. optimally active values 5.7 or below. These enzymes play an essential role stepwise conversion brain. It is suggested that they are involved modulation central activities ACTH
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