Naraparaju V R, Yamamoto N
Albert Einstein Cancer Center, Philadelphia, PA 19141.
Immunol Lett. 1994 Dec;43(3):143-8. doi: 10.1016/0165-2478(94)90214-3.
The outer surface of mouse B lymphocytes carries constitutive and inducible beta-galactosidase isozymes. A brief (30 min) treatment of B lymphocytes with lysophosphatidylcholine (lyso-Pc) immediately induced an approximate 3-fold higher beta-galactosidase activity than the constitutive isozyme of untreated B lymphocytes. Thus, the lyso-Pc-inducible isozyme is not a de novo enzyme. Outer surface of mouse T lymphocytes carries constitutive (non-Neu-1) and inducible (Neu-1) sialidase isozymes. The lyso-Pc-inducible beta-galactosidase of B lymphocytes and the Neu-1 sialidase of T lymphocytes were required for conversion of vitamin D3-binding protein (Gc protein) to a potent macrophage activating factor. This enzymatic generation of the macrophage activating factor was mediated via enzyme-associated receptors.
小鼠B淋巴细胞的外表面携带着组成型和诱导型β-半乳糖苷酶同工酶。用溶血磷脂酰胆碱（lyso-Pc）对B淋巴细胞进行短暂（30分钟）处理，立即诱导出的β-半乳糖苷酶活性比未处理的B淋巴细胞的组成型同工酶高约3倍。因此，lyso-Pc诱导型同工酶不是一种从头合成的酶。小鼠T淋巴细胞的外表面携带着组成型（非Neu-1）和诱导型（Neu-1）唾液酸酶同工酶。B淋巴细胞的lyso-Pc诱导型β-半乳糖苷酶和T淋巴细胞的Neu-1唾液酸酶是将维生素D3结合蛋白（Gc蛋白）转化为强效巨噬细胞激活因子所必需的。巨噬细胞激活因子的这种酶促生成是通过酶相关受体介导的。
