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核心技术专利：CN118964589B侵权必究

核心技术专利：CN118964589B侵权必究

de Souza A N, Bruno J A, Carvalho K M

Departamento de Fisiologia e Farmacologia, CCS da Universidade Federal do Ceara, Brazil.

Comp Biochem Physiol C Comp Pharmacol Toxicol. 1991;99(3):363-7. doi: 10.1016/0742-8413(91)90257-t.

A soluble human brain aminopeptidase which hydrolyses the Tyr-Gly bond of Met-enkephalin and Leu-enkephalin was identified in the brains of the following vertebrates: mammals (Callithrix jacchus and Rattus norvegicus), bird (Gallus domesticus), reptile (Tupinambis teguixin), amphibia (Bufo paracnemis), fish (Sarotherdon niloticus) and elasmobranchy (Galeocerdo cuvieri). 2. The properties of this enzyme are: molecular weight near 100,000 Da, isoelectric point near 4.9, optimum pH near 7.5, activation by dithiothreitol, strong inhibition by Cu2+, Zn2+, Ni2+, puromycin and bacitracin, hydrolysis of enkephalins and basic and neutral aminoacid-beta-naphythylamide substrates. 3. The results indicate the preservation of this human brain aminopeptidase during the course of vertebrate phylogeny.

de Souza A N, Bruno J A, Carvalho K M

Departamento de Fisiologia e Farmacologia, CCS da Universidade Federal do Ceara, Brazil.

Comp Biochem Physiol C Comp Pharmacol Toxicol. 1991;99(3):363-7. doi: 10.1016/0742-8413(91)90257-t.

A soluble human brain aminopeptidase which hydrolyses the Tyr-Gly bond of Met-enkephalin and Leu-enkephalin was identified in the brains of the following vertebrates: mammals (Callithrix jacchus and Rattus norvegicus), bird (Gallus domesticus), reptile (Tupinambis teguixin), amphibia (Bufo paracnemis), fish (Sarotherdon niloticus) and elasmobranchy (Galeocerdo cuvieri). 2. The properties of this enzyme are: molecular weight near 100,000 Da, isoelectric point near 4.9, optimum pH near 7.5, activation by dithiothreitol, strong inhibition by Cu2+, Zn2+, Ni2+, puromycin and bacitracin, hydrolysis of enkephalins and basic and neutral aminoacid-beta-naphythylamide substrates. 3. The results indicate the preservation of this human brain aminopeptidase during the course of vertebrate phylogeny.