Catalytic properties of three L-lactate dehydrogenases from saffron corms (Crocus sativus L.)

Molecular Biology Reports

Volumn 29, Issue 1-2, 2002, Pages 163-166

  Keyhani, Ezzatollah ^a,b   Sattarahmady, Naghmeh ^b  

^a Laboratory for Life Sciences   (Iran)

^b UNIVERSITY OF TEHRAN   (Iran)

Author keywords

[No Author keywords available]

Indexed keywords

CROCUS SATIVUS;

CYTOCHROME; FERRICYANIDE; ISOENZYME; LACTATE DEHYDROGENASE;

ARTICLE; CATALYSIS; CROCUS; ELECTRON TRANSPORT; ENZYMOLOGY; KINETICS; METABOLISM; OXIDATION REDUCTION REACTION; PH; PLANT;

CATALYSIS; CROCUS; CYTOCHROMES; ELECTRON TRANSPORT; FERRICYANIDES; HYDROGEN-ION CONCENTRATION; ISOENZYMES; KINETICS; L-LACTATE DEHYDROGENASE; OXIDATION-REDUCTION; PLANT COMPONENTS;

EID: 0036042118     PISSN: 03014851     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1020365526792     Document Type: Article

References (11)

1. 2: Kinetic studies by absorbance and electron-paramagnetic-resonance spectroscopy of electron distribution among prosthetic groups
2. Utilization by yeast of D-lactate and L-lactate as sources of energy in the presence of antimycin A
3. 2 and oxidized cytochrome c
4. 2 de Saccharomyces cerevisiae
5. 2 at 2.4 Å resolution
6. 2 from baker's yeast
7. 2 mutant crystallized in the presence of lactate or phenyl lactate
8. 2: Comparison with the intact wild-type enzyme
9. Practical limits and prospects (kinetics)
10. L-Lactate dehydrogenase from leaves of higher plants
11. Catalytic properties of three lactate dehydrogenases from potato tubers (Solanum tuberosum)