Human colon sialidase: characterization and activity levels in normal mucosa and colonic adenocarcinoma.

Enzyme & protein Pub Date : 1994-01-01 DOI:10.1159/000475001
V S Martínez-Zorzano, C Feijoo, M Páez de la Cadena, M Butrón, A Fernández-Briera, F J Rodríguez-Berrocal
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引用次数: 4

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).

人结肠唾液酸酶:在正常粘膜和结肠腺癌中的特征和活性水平。
人类结肠唾液酸酶已被表征,其在正常粘膜和结肠腺癌中的活性水平已被确定。唾液酸酶在pH为5.5时活性最高,在4℃和-20℃时不稳定,大部分活性与颗粒相关,与triton X-100或3-([3-胆酰胺丙基]-二甲胺)-1-丙砜均不能释放。以2′-(4-methylumbelliferyl) α - d - n -乙酰神经氨酸为底物,Km和Vmax分别为0.140 mmol/l和63 mU/g。此外,检测到底物浓度高于1.5 mmol/l的抑制作用。神经氨酸在Ki为3.5 mmol/l时产生竞争性抑制。原发性结肠腺癌组织唾液酸酶特异性活性(104.20 +/- 8.00 mU/g)高于正常黏膜组织(72.50 +/- 7.67 mU/g),差异有统计学意义(p < 0.001)。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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