作者: Anthony P. Corfield , Susan A. Wagner , Luke J. D. O'Donnell , Paul Durdey , Richard A. Mountford
DOI: 10.1007/BF00731190
关键词: Oligosaccharide 、 Glycosulfatase activity 、 Biochemistry 、 Esterase 、 Sialidase 、 Sialic acid 、 Acetylesterase 、 Biology 、 Glycosulfatase 、 Sialate O-acetylesterase
摘要: Sialidase activity in normal faecal extracts showed a preference for mucin-related glycoprotein and oligosaccharide substrates, but the presence of two or moreO-acetyl esters at positions C7–C9 on sialic acids retarded rate hydrolysis. A specific sialateO-acetyl esterase was detected with lower total relative to sialidase mucin substrates having pH optimum 7.8 aKM approximately 1mm ester. glycosulfatase found using substrate lactit-[3H]ol 6-O-sulfate 5.0 1mm.