作者: Z Glatz , J Kovár , L Macholán , P Pec
DOI: 10.1042/BJ2420603
关键词:
摘要: Diamine oxidase was prepared from pea (Pisum sativum) seedlings by a new purification procedure involving two h.p.l.c. steps. We studied the optical and electrochemical properties of homogeneous enzyme also analysed hydrolysed protein several methods. The data presented here suggest that carbonyl cofactor diamine is firmly bound pyrroloquinoline quinone.