Enzymatic and thermodynamic profiles of a heterotetramer lactate dehydrogenase isozyme in swine.
Biochem Biophys Res Commun
; 479(4): 860-867, 2016 Oct 28.
Article
en En
| MEDLINE
| ID: mdl-27671200
Palabras clave
H(2)M(2); HCQ; Heterotetrameric isozyme; Hydroxychloroquine; K(m); LDH; Lactate dehydrogenase; T(half); T(max); V(max); heterotetrameric lactate dehydrogenase isozyme consisting of two LDHA-encoded muscle type and two LDHB-encoded heart muscle type molecules; hydroxychloroquine; lactate dehydrogenase; optimum temperature for LDH pyruvate reduction activity; residual activity of LDH pyruvate reduction activity; van't Hoff enthalpy
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Porcinos
/
L-Lactato Deshidrogenasa
Límite:
Animals
Idioma:
En
Revista:
Biochem Biophys Res Commun
Año:
2016
Tipo del documento:
Article
País de afiliación:
Japón
Pais de publicación:
Estados Unidos