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Natural variation in enzyme activity of the African cichlid Pseudocrenilabrus multicolor victoriae

Authors :
Crocker, Cindy D.
Chapman, Lauren J.
Martínez, Mery L.
Source :
Comparative Biochemistry & Physiology - Part B: Biochemistry & Molecular Biology. Jan2013, Vol. 164 Issue 1, p53-60. 8p.
Publication Year :
2013

Abstract

Abstract: This study describes the metabolic capacities of the African cichlid Pseudocrenilabrus multicolor victoriae from four sites in Uganda, East Africa. Fish were captured during the dry season, from two aquatic systems in different regions (Lake Nabugabo and Mpanga River). Within the Lake Nabugabo region, individuals were sampled from Lake Kayanja (normoxic) and Lwamunda Swamp (hypoxic); within the Mpanga River system, individuals were sampled from Bunoga and Kahunge (characterized by seasonal variation in dissolved oxygen (D.O.)). Enzyme activity levels of pyruvate kinase, lactate dehydrogenase, citrate synthase, and cytochrome C oxidase were measured in four tissues: white skeletal muscle, heart, brain, and liver. Two additional enzymes were measured in the liver, malate dehydrogenase and fructose 1,6-bisphosphatase. Regional differences between enzyme activities in most tissues were evident; however, little variation was observed between two sites within a region despite differences in D.O. In general, P. multicolor from the Mpanga River system displayed greater anaerobic enzyme activity in white skeletal muscle, lower gluconeogenic enzyme activity in the liver, and an overall higher enzyme activity in the heart and brain tissues than fish from the Nabugabo region. The latter may reflect a long-term adaptation to low-oxygen conditions at the metapopulation level in the Nabugabo region. [Copyright &y& Elsevier]

Details

Language :
English
ISSN :
10964959
Volume :
164
Issue :
1
Database :
Academic Search Index
Journal :
Comparative Biochemistry & Physiology - Part B: Biochemistry & Molecular Biology
Publication Type :
Academic Journal
Accession number :
83873256
Full Text :
https://doi.org/10.1016/j.cbpb.2012.10.003