Biochemical properties of carboxypeptidase fromAloe arborescens Miller var.natalensis Berger

Autor:	Hidehiko Beppu, Masafumi Obata, Shosuke Ito, Ryo Teradaira, Keisuke Fujita, Toshiharu Nagatsu
Rok vydání:	1993
Předmět:	Pharmacology chemistry.chemical_classification biology Stereochemistry Liliaceae Biological activity Pharmacognosy biology.organism_classification Carboxypeptidase Enzyme Serine carboxypeptidase chemistry Biochemistry biology.protein Aloe arborescens Proline
Zdroj:	Phytotherapy Research. 7:S26-S29
ISSN:	1099-1573 0951-418X
DOI:	10.1002/ptr.2650070710
Popis:	A carboxypeptidase was partially purified from Aloe arborescens Miller var. natalensis Berger on a scale suitable for pharmacological studies. The enzyme was most active and stable at pH 5.0. The enzyme had a broad specificity against various synthetic peptides, being capable of splitting C-terminal proline. Its activity was inhibited almost completely by diisopropylfluorophosphate, strongly by transition metals, such as Fe 3+ , Hg 2+ and Cu 2+ , and moderately by sulphydryl reagents. These results indicate that Aloe enzyme is a serine carboxypeptidase and appears to contain a sulphydryl group that may be involved in its inactivation
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::40a73e376c57611831056725f50bc882 https://doi.org/10.1002/ptr.2650070710 Zobrazit plný text záznamu Plný text