Thermal behavior of a lactate dehydrogenase purified from the heterothermic and sympatric vertebrate species brook lamprey (Lampetra planeri), tench (Tenca tenca), smooth (Triturus vulgaris) and alpine newt (Triturus alpestris)

Alessandro Ferracin, Margherita Annicchiarico, Annamaria Coscarella, Angela Teichner, Massimo Dell'Agata

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Abstract

1. 1. The A4 lactate dehydrogenase isozyme was purified to homogeneity from the tissues of Brook lamprey (Lampetra planeri) tench (Tenca tenca), smooth newt (Triturus vulgaris) and alpine newt (T. alpestris). 2. 2. These four species share their geographical distribution in the same freshwater habitats, often live together in the same station and two of them are congeneric. Steady-state kinetic investigations have shown that: 3. 3. Km (apparent) for pyruvate vs. temperature and (apparent) product Ki (Pyruvate) and Ki (Lactate) are fairly similar among species; 4. 4. kcat/Km decreases with temperature in the case of the newts but increases in the case of both lamprey and tench; 5. 5. Thermostability does not correlate to preferred ambient temperature and, in particular, tench LDH starts being inactivated up to 65°C. 6. 6. Thermostability does not correlate with activation energy either; 7. 7. No clear relationships can be demonstrated either between activation energy and conformational transitions in the molecule (these latter indicated by breaks in the Arrhenius plots) nor between activation energy and molecular flexibility, investigated by melting experiments.

Original languageEnglish
Pages (from-to)435-443
Number of pages9
JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volume94
Issue number3
DOIs
Publication statusPublished - 1989

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Triturus
Sympatry
Lampreys
Salamandridae
Cyprinidae
L-Lactate Dehydrogenase
Vertebrates
Activation energy
Hot Temperature
Pyruvic Acid
Temperature
Geographical distribution
Arrhenius plots
Fresh Water
Freezing
Isoenzymes
Ecosystem
Lactic Acid
Melting
Tissue

ASJC Scopus subject areas

  • Medicine(all)

Cite this

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title = "Thermal behavior of a lactate dehydrogenase purified from the heterothermic and sympatric vertebrate species brook lamprey (Lampetra planeri), tench (Tenca tenca), smooth (Triturus vulgaris) and alpine newt (Triturus alpestris)",
abstract = "1. 1. The A4 lactate dehydrogenase isozyme was purified to homogeneity from the tissues of Brook lamprey (Lampetra planeri) tench (Tenca tenca), smooth newt (Triturus vulgaris) and alpine newt (T. alpestris). 2. 2. These four species share their geographical distribution in the same freshwater habitats, often live together in the same station and two of them are congeneric. Steady-state kinetic investigations have shown that: 3. 3. Km (apparent) for pyruvate vs. temperature and (apparent) product Ki (Pyruvate) and Ki (Lactate) are fairly similar among species; 4. 4. kcat/Km decreases with temperature in the case of the newts but increases in the case of both lamprey and tench; 5. 5. Thermostability does not correlate to preferred ambient temperature and, in particular, tench LDH starts being inactivated up to 65°C. 6. 6. Thermostability does not correlate with activation energy either; 7. 7. No clear relationships can be demonstrated either between activation energy and conformational transitions in the molecule (these latter indicated by breaks in the Arrhenius plots) nor between activation energy and molecular flexibility, investigated by melting experiments.",
author = "Alessandro Ferracin and Margherita Annicchiarico and Annamaria Coscarella and Angela Teichner and Massimo Dell'Agata",
year = "1989",
doi = "10.1016/0305-0491(89)90178-8",
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AU - Ferracin, Alessandro

AU - Annicchiarico, Margherita

AU - Coscarella, Annamaria

AU - Teichner, Angela

AU - Dell'Agata, Massimo

PY - 1989

Y1 - 1989

N2 - 1. 1. The A4 lactate dehydrogenase isozyme was purified to homogeneity from the tissues of Brook lamprey (Lampetra planeri) tench (Tenca tenca), smooth newt (Triturus vulgaris) and alpine newt (T. alpestris). 2. 2. These four species share their geographical distribution in the same freshwater habitats, often live together in the same station and two of them are congeneric. Steady-state kinetic investigations have shown that: 3. 3. Km (apparent) for pyruvate vs. temperature and (apparent) product Ki (Pyruvate) and Ki (Lactate) are fairly similar among species; 4. 4. kcat/Km decreases with temperature in the case of the newts but increases in the case of both lamprey and tench; 5. 5. Thermostability does not correlate to preferred ambient temperature and, in particular, tench LDH starts being inactivated up to 65°C. 6. 6. Thermostability does not correlate with activation energy either; 7. 7. No clear relationships can be demonstrated either between activation energy and conformational transitions in the molecule (these latter indicated by breaks in the Arrhenius plots) nor between activation energy and molecular flexibility, investigated by melting experiments.

AB - 1. 1. The A4 lactate dehydrogenase isozyme was purified to homogeneity from the tissues of Brook lamprey (Lampetra planeri) tench (Tenca tenca), smooth newt (Triturus vulgaris) and alpine newt (T. alpestris). 2. 2. These four species share their geographical distribution in the same freshwater habitats, often live together in the same station and two of them are congeneric. Steady-state kinetic investigations have shown that: 3. 3. Km (apparent) for pyruvate vs. temperature and (apparent) product Ki (Pyruvate) and Ki (Lactate) are fairly similar among species; 4. 4. kcat/Km decreases with temperature in the case of the newts but increases in the case of both lamprey and tench; 5. 5. Thermostability does not correlate to preferred ambient temperature and, in particular, tench LDH starts being inactivated up to 65°C. 6. 6. Thermostability does not correlate with activation energy either; 7. 7. No clear relationships can be demonstrated either between activation energy and conformational transitions in the molecule (these latter indicated by breaks in the Arrhenius plots) nor between activation energy and molecular flexibility, investigated by melting experiments.

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