Ohkubo I, Gasa S, Namikawa C, Makita A, Sasaki M
Department of Biochemistry, Nagoya City University Medical School, Japan.
Biochem Biophys Res Commun. 1991 Feb 14;174(3):1133-40. doi: 10.1016/0006-291x(91)91538-n.
Chymotrypsin-like activity of multicatalytic proteinase (MCP) purified from human erythrocytes was selectively activated 2.5--3.5-fold by sulfated glycolipids such as galactosylceramide sulfate (SM4) and lactosylceramide sulfate (SM3) but not by other glycolipids including galactosylceramide (GalCer), lactosylceramide (LacCer), GD1a, GM1 and GM3. Heparin also selectively activated trypsin-like activity 2.5-fold, while other mucopolysaccharides did not. This proteinase molecule bound specifically and with high affinity to both SM4 and SM3, but not to GalCer, LacCer and GM3. The binding of SM4 and SM3 to the enzyme molecule was also confirmed by thin layer chromatography.
从人红细胞中纯化得到的多催化蛋白酶（MCP）的胰凝乳蛋白酶样活性可被硫酸化糖脂如硫酸半乳糖神经酰胺（SM4）和硫酸乳糖神经酰胺（SM3）选择性激活2.5至3.5倍，而其他糖脂包括半乳糖神经酰胺（GalCer）、乳糖神经酰胺（LacCer）、GD1a、GM1和GM3则无此作用。肝素也能选择性激活胰蛋白酶样活性2.5倍，而其他粘多糖则不能。该蛋白酶分子与SM4和SM3均能特异性且高亲和力结合，但与GalCer、LacCer和GM3不结合。通过薄层色谱法也证实了SM4和SM3与酶分子的结合。
