Podhajcer O L, Filmus J E, Mordoh J
Mol Cell Biochem. 1985 Feb;66(1):39-43. doi: 10.1007/BF00231821.
The presence of a prostatic-like acid phosphatase is reported in human lactating milk. Its activity is associated with skim milk and it could be separated from the other acid phosphatases only after Triton X-100 treatment. By all the criteria applied, it appears to be very similar to prostatic acid phosphatase. An approximate molecular weight of 96 000 was measured for the native enzyme, which is inhibited by L-(+)tartrate and has similar electrophoretic migration. Besides, it hydrolyzes choline-o-phosphate very well and cross-reacts with an antibody anti-prostatic acid phosphatase. This prostatic-like acid phosphatase has also been detected in a human mammary carcinoma from a lactating patient.
据报道,人乳汁中存在一种前列腺样酸性磷酸酶。其活性与脱脂乳相关,并且只有在经 Triton X - 100 处理后才能与其他酸性磷酸酶分离。根据所应用的所有标准,它似乎与前列腺酸性磷酸酶非常相似。测得天然酶的近似分子量为 96000,它可被 L-(+)酒石酸盐抑制,且具有相似的电泳迁移率。此外,它能很好地水解磷酸胆碱,并与抗前列腺酸性磷酸酶抗体发生交叉反应。在一名哺乳期患者的人乳腺癌中也检测到了这种前列腺样酸性磷酸酶。