Biochemical properties of carboxypeptidase from  Aloe arborescens  Miller var.  natalensis  Berger | Zendy

Ito Shosuke | Zendy; Teradaira Ryo | Zendy; Beppu Hidehiko | Zendy; Obata Masafumi | Zendy; Fujita Keisuke | Zendy; Nagatsu Toshiharu | Zendy

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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.

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