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Biogenic Polyamines Affect Activity of Aminopeptidase B and Alanyl Aminopeptidase from Porcine Skeletal Muscle
Author(s) -
FLORES MÓNICA,
ARISTOY MCONCEPCIÓN,
TOLDRÁ FIDEL
Publication year - 1996
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1996.tb14715.x
Subject(s) - cadaverine , putrescine , spermidine , agmatine , spermine , aminopeptidase , biochemistry , polyamine , chemistry , enzyme , biogenic amine , tyramine , leucine , amino acid , serotonin , receptor
The effect of biogenic polyamines (agmatine, cadaverine, putrescine, spermidine, and spermine) on the activity of pork muscle aminopeptidase and alanyl aminopeptidase was investigated. Agmatine (5 mM) showed a powerful inhibitory effect for both enzymes (more than 50% inhibition). Cadaverine and less intensely putrescine showed similar inhibitory effects for both enzymes. All assayed polyamines inhibited activity of both aminopeptidases except spermine and spermidine which did not affect aminopeptidase B. Thus, one of these inhibitors could be used to avoid the interference of alanyl aminopeptidase when assaying aminopeptidase B in muscle extracts.