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Inhibition effects of some pesticides and heavy metals on carbonic anhydrase enzyme activity purified from horse mackerel (Trachurus trachurus) gill tissues.

Authors :
Caglayan, Cuneyt
Taslimi, Parham
Türk, Cebrahil
Gulcin, İlhami
Kandemir, Fatih Mehmet
Demir, Yeliz
Beydemir, Şükrü
Source :
Environmental Science & Pollution Research; Apr2020, Vol. 27 Issue 10, p10607-10616, 10p
Publication Year :
2020

Abstract

The gill tissue is the main site of metabolic enzymes or compensation, with the kidney tissue playing a supporting role. At the gill tissue, carbonic anhydrase enzymes (CAs) catalyze the hydration of CO<subscript>2</subscript> to HCO<subscript>3</subscript><superscript>−</superscript> and H<superscript>+</superscript> for production to the H<subscript>2</subscript>O. In this work, the CA enzyme was purified from horse mackerel (Trachurus trachurus) gill with a specific activity of 21,381.42 EU/mg, purification fold of 150.61, total activity of 2347.68 EU/mL, and a yield of 16.13% using sepharose 4B-L-tyrosine-sulfanilamide affinity gel chromatography. For recording the enzyme purity, gel electrophoresis was performed, and single band was seen. The molecular weight of this enzyme was found approximately 35 kDa. Also, the inhibitory effects of different pesticides such as thiram, clofentezine, propineb, deltamethrin, azoxystrobin, and thiophanate and heavy metal ions such as Fe<superscript>2+</superscript>, Cu<superscript>2+</superscript>, Co<superscript>2+</superscript>, Pb<superscript>2+</superscript> Hg<superscript>2+</superscript>, and As<superscript>3+</superscript> on horse mackerel gill tissue CA enzyme activities were investigated. Our results indicated that these pesticides and metal ions showed inhibitory effects at low nanomolar and millimolar concentrations for fish gill CA enzymes, respectively. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
09441344
Volume :
27
Issue :
10
Database :
Complementary Index
Journal :
Environmental Science & Pollution Research
Publication Type :
Academic Journal
Accession number :
142533778
Full Text :
https://doi.org/10.1007/s11356-020-07611-z