Studies of rabbit brain, intestine and liver guanine aminohydrolase.
Comp Biochem Physiol B
; 77(3): 619-27, 1984.
Article
en En
| MEDLINE
| ID: mdl-6713831
ABSTRACT
Guanine aminohydrolase (EC 3.5.4.3) from rabbit brain, intestine, and liver has been purified to homogeneity by affinity chromatography at room temperature and 0-4 degrees C. In all cases the recovery and fold purification was greatest for purification at room temperature. Each enzyme has a subunit mol. wt of 49,500 and crosslinking studies revealed the native form to be a dimer. The amino acid analysis showed a high content of asx, glx, ser, gly and leu; the pI was 5.0 for each prep. The Michaelis constants at pH 8.0 were 6.1, 6.1 and 5.8 X 10(-6) M for brain, intestine and liver GAH respectively. The enzymes had a broad pH activity profile with an optimum of pH 8.0-8.5.
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Banco de datos:
MEDLINE
Asunto principal:
Encéfalo
/
Aminohidrolasas
/
Guanina Desaminasa
/
Intestinos
/
Hígado
Límite:
Animals
Idioma:
En
Revista:
Comp Biochem Physiol B
Año:
1984
Tipo del documento:
Article