Theses and Dissertations


Title: Lactate dehydrogenase isozymes of Nile tilapia (Tilapia nilotica), Java tilapia (Tilapia mossambica) and their reciprocal crosses

Name: Lankford III, John Christopher

Degree: MS

Chair: Dr. E.W. Shell

Resides: FAA Library

University: Auburn

Location: Auburn, Alabama

Date: 1966

Pages: 45

Keywords: Lactate Dehydrogenase Isozymes,Nile Tilapia,Tilapia nilotica,Java Tilapia,Tilapia mossambica,Reciprocal Crosses.

Abstract:

The lactate dehydrogenase isozymes of Nile tilapia (Tilapia nilotica), Java tilapia (Tilapia mossambica) and their reciprocal crosses were investigated using acrylamide gel electrophoresis, gel filtration and spectrophotometry. Separations of isozymes on acrylamide gels revealed a total of eight electrophoretically distinct forms. No difference was found in isozyme patterns from brain, heart, liver, skeletal muscle, ovaries or testes of the parent species and their genotypes. The two-dimensional electrophoresis separation of Nile tilapia brain LDH isozymes was linear. Molecular weight determinations on Bio-Gel P-150 columns demonstrated that Nile tilapia heart LDH isozymes approximate a molecular size of 135,000 g/mole. Kinetics studies on pyruvate inhibition of heart and liver LDH's indicated the sensitivity of these organs to pyruvate accumulation. Assays of skeletal muscle LDH's confirmed the affinity of this tissue for high pyruvate concentrations. The optimum substrate concentration for skeletal muscle (2.1 x 10-3 M) was 4 times greater than the optimum concentration for liver and heart isozymes. Brain LDH isozymes were not affected by increasing substrate concentration as was skeletal muscle: however, optimum substrate concentrations were more like those of liver and heart LDH's.

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