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 language | English |
|---|---|
| Pages (from-to) | 435-443 |
| Number of pages | 9 |
| Journal | Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology |
| Volume | 94 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 1989 |
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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). / Ferracin, Alessandro; Annicchiarico, Margherita; Coscarella, Annamaria; Teichner, Angela; Dell'Agata, Massimo.
In: Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology, Vol. 94, No. 3, 1989, p. 435-443.Research output: Contribution to journal › Article
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TY - JOUR
T1 - 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)
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.
UR - http://www.scopus.com/inward/record.url?scp=0024848472&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0024848472&partnerID=8YFLogxK
U2 - 10.1016/0305-0491(89)90178-8
DO - 10.1016/0305-0491(89)90178-8
M3 - Article
C2 - 2620488
AN - SCOPUS:0024848472
VL - 94
SP - 435
EP - 443
JO - Comparative Biochemistry and Physiology Part - B: Biochemistry and Molecular Biology
JF - Comparative Biochemistry and Physiology Part - B: Biochemistry and Molecular Biology
SN - 1096-4959
IS - 3
ER -