Identification and characterization of a novel zebrafish (Danio rerio) pentraxin-carbonic anhydrase.

ABSTRACT:

Background

Carbonic anhydrases (CAs) are ubiquitous, essential enzymes which catalyze the conversion of carbon dioxide and water to bicarbonate and H⁺ ions. Vertebrate genomes generally contain gene loci for 15-21 different CA isoforms, three of which are enzymatically inactive. CA VI is the only secretory protein of the enzymatically active isoforms. We discovered that non-mammalian CA VI contains a C-terminal pentraxin (PTX) domain, a novel combination for both CAs and PTXs.

Methods

We isolated and sequenced zebrafish (Danio rerio) CA VI cDNA, complete with the sequence coding for the PTX domain, and produced the recombinant CA VI-PTX protein. Enzymatic activity and kinetic parameters were measured with a stopped-flow instrument. Mass spectrometry, analyt

SUBMITTER: Patrikainen MS 

PROVIDER: S-EPMC5723433 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature