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Biochemical properties of carboxypeptidase from Aloe arborescens Miller var. natalensis Berger
Author(s) -
Ito Shosuke,
Teradaira Ryo,
Beppu Hidehiko,
Obata Masafumi,
Fujita Keisuke,
Nagatsu Toshiharu
Publication year - 1993
Publication title -
phytotherapy research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.019
H-Index - 129
eISSN - 1099-1573
pISSN - 0951-418X
DOI - 10.1002/ptr.2650070710
Subject(s) - carboxypeptidase , enzyme , serine , proline , biochemistry , carboxypeptidase a , chemistry , reagent , biology , stereochemistry , amino acid , organic chemistry
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.