Human colon sialidase: characterization and activity levels in normal mucosa and colonic adenocarcinoma.
Enzyme Protein
; 48(5-6): 282-90, 1994.
Article
en En
| MEDLINE
| ID: mdl-8792873
ABSTRACT
Human colon sialidase has been characterized, and its activity levels in normal mucosa and colonic adenocarcinoma have been determined. Sialidase activity was maximal at pH 5.5, and was unstable with storage at 4 and -20 degrees C. The bulk of activity was pellet-associated, and could not be released with triton X-100 or 3-([3-cholamidopropyl]- dimethylammonio)-1-propanesulfonate. Using 2'-(4-methylumbelliferyl)alpha-D-N-acetylneuraminic acid as substrate, the Km and Vmax values were estimated to be 0.140 mmol/l and 63 mU/g, respectively. Furthermore, an inhibition by substrate concentrations above 1.5 mmol/l was detected. Neuraminic acid caused a competitive inhibition with a Ki of 3.5 mmol/l. A statistically significant increase (p < 0.001) in the sialidase specific activity was found in primary colonic adenocarcinoma (104.20 +/- 8.00 mU/g) compared to that of the normal mucosa (72.50 +/- 7.67 mU/g).
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Banco de datos:
MEDLINE
Asunto principal:
Himecromona
/
Adenocarcinoma
/
Colon
/
Neoplasias del Colon
/
Neuraminidasa
Tipo de estudio:
Diagnostic_studies
Límite:
Humans
Idioma:
En
Revista:
Enzyme Protein
Asunto de la revista:
BIOQUIMICA
Año:
1994
Tipo del documento:
Article
País de afiliación:
España