Properties of a cryptic lysyl oxidase from haloarchaeon Haloterrigena turkmenica.

ABSTRACT:

Background

Lysyl oxidases (LOX) have been extensively studied in mammals, whereas properties and functions of recently found homologues in prokaryotic genomes remain enigmatic.

Methods

LOX open reading frame was cloned from Haloterrigena turkmenica in an E. coli expression vector. Recombinant Haloterrigena turkmenica lysyl oxidase (HTU-LOX) proteins were purified using metal affinity chromatography under denaturing conditions followed by refolding. Amine oxidase activity has been measured fluorometrically as hydrogen peroxide release coupled with the oxidation of 10-acetyl-3,7-dihydroxyphenoxazine in the presence of horseradish peroxidase. Rabbit polyclonal antibodies were obtained and used in western blotting.

Results

Cultured H. turkmenica

SUBMITTER: Pestov NB 

PROVIDER: S-EPMC6452851 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature