发育中鸡胚肝脏酸性磷酸酶的异质性
Heterogeneity of liver acid phosphatases in developing chick embryo.
作者信息
Wang K M
出版信息
Biochem J. 1969 Nov;115(2):191-7. doi: 10.1042/bj1150191.
Abstract
- The development, localization and heterogeneity of acid phosphatase and a Zn(2+)-activated acid phosphatase in cellular fractions of developing chick liver were studied. 2. Acid phosphatase is distributed abundantly in the particulate and soluble fractions. The soluble fraction is rich in Zn(2+)-activated acid phosphatase, which attains its peak activity at about 15 days of incubation. 3. The particulate acid phosphatase activity is inhibited by fluoride but not by sodium l(+)-tartrate or cysteine. On the other hand, the soluble Zn(2+)-activated acid phosphatase activity is inhibited by sodium l(+)-tartrate and cysteine but not by fluoride. 4. The pH optimum of these two enzymes is similar at about 5.6. 5. The soluble Zn(2+)-activated acid phosphatase activity appears to be thermally stabilized by the treatment with Triton X-100 or bovine serum albumin.
摘要
- 研究了发育中的鸡肝脏细胞组分中酸性磷酸酶和锌（2+）激活的酸性磷酸酶的发育、定位和异质性。2. 酸性磷酸酶大量分布于颗粒组分和可溶组分中。可溶组分富含锌（2+）激活的酸性磷酸酶，其在孵育约15天时达到峰值活性。3. 颗粒酸性磷酸酶活性受氟化物抑制，但不受L（+）-酒石酸钠或半胱氨酸抑制。另一方面，可溶锌（2+）激活的酸性磷酸酶活性受L（+）-酒石酸钠和半胱氨酸抑制，但不受氟化物抑制。4. 这两种酶的最适pH值相似，约为5.6。5. 用 Triton X-100 或牛血清白蛋白处理后，可溶锌（2+）激活的酸性磷酸酶活性似乎得到热稳定。
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