Korngold L
Int Arch Allergy Appl Immunol. 1977;54(4):300-7. doi: 10.1159/000231841.
Human kidney alkaline phosphatase (AP) react with antisera to liver and intestinal AP. The respective kidney enzymes are designated as KLi and KI. Comparison with liver AP showed that KLi was salted out at the same ammonium sulfate concentration (66%) as the liver enzyme; KLi was antigenically identical with liver AP; the electrophoretic mobility of KLi was that of a gamma-globulin whereas liver AP was an alpha2-globulin. the liver enzyme was lighter (130,000 daltons) than KLi (150,000 daltons). KI and intestinal AP shared most properties: antigenically they were indistinguishable; both contained two components one of which was 80,000 daltons, the other was heavier (120,000 daltons for KI, 130,000 daltons for intestinal AP). Urinary AP consisted only of the lighter component (80,000 dalton). Methods for partial separation of the three kidney APs are given.
人肾碱性磷酸酶（AP）与抗肝和抗肠AP血清发生反应。各自的肾酶分别命名为KLi和KI。与肝AP比较表明，KLi与肝酶在相同的硫酸铵浓度（66%）下盐析；KLi与肝AP抗原性相同；KLi的电泳迁移率显示其为γ球蛋白，而肝AP为α2球蛋白。肝酶（130,000道尔顿）比KLi（150,000道尔顿）轻。KI和肠AP具有大多数共同特性：抗原性上无法区分；两者都含有两个组分，其中一个为80,000道尔顿，另一个较重（KI为120,000道尔顿，肠AP为130,000道尔顿）。尿AP仅由较轻的组分（80,000道尔顿）组成。文中给出了三种肾AP部分分离的方法。
