Tseng C C, Tseng E E, Sensibar J A, Lee C
Prostate. 1986;9(1):57-64. doi: 10.1002/pros.2990090109.
Properties of acid phosphatase in the rat ventral prostate were compared with those in seven other organs in adult male rats by the electrophoretic mobility in acrylamide gels, susceptibility to reactions with inhibitors, and by their response to castration and subsequent testosterone replacement. The enzyme in the spleen exhibited the highest values of Km and Vmax. These values in the prostate, the liver, and the kidney showed an intermediate level, while the lowest level was found in the heart, the lung, the adrenals, and the seminal vesicle. Upon electrophoresis, a total of six isoenzyme bands were resolved. Two major zones of activity were noted. They were the slow-moving anodal bands (isoenzymes 1,2, and 3) and the fast-moving cathodal bands (isoenzymes 4,5, and 6). The spleen possessed the highest number of isoenzymes (bands 1,2,4,5 and 6) and the prostate had three (bands 1,2, and 3). The heart contained only one (band 2). Two isoenzymes (bands 1 and 2) were found in remaining organs. Results of the effects of inhibitors showed that NaF inhibited all six isoenzymes, while L(+)tartrate inhibited mainly those in the anodal zone. D(-)tartrate and formaldehyde showed no significant inhibition to any of the isoenzymes. PCMB (para-chloromercuribenzoic acid) was found to be a specific inhibitor for isoenzyme 3. Upon castration in the hosts, the enzyme activity in the prostate, the liver, and the seminal vesicle was significantly reduced. This reduction in enzyme activity involved all isoenzymes in these three organs, but isoenzyme 3 in the prostate disappeared completely after castration. The activities of these isoenzymes were restored by testosterone replacement. These results indicate that acid phosphatase in rat tissues has multiple forms; each has its own electrophoretic mobility in acrylamide gels, sensitivity to inhibitors, and response to hormonal manipulation. Isoenzyme 3 is specific to the prostate and is uniquely sensitive to PCMB inhibition and to androgen stimulation.
通过在丙烯酰胺凝胶中的电泳迁移率、与抑制剂反应的敏感性以及对去势和随后睾酮替代的反应，比较了成年雄性大鼠腹侧前列腺中酸性磷酸酶的特性与其他七个器官中的特性。脾脏中的酶表现出最高的Km和Vmax值。前列腺、肝脏和肾脏中的这些值处于中间水平，而心脏、肺、肾上腺和精囊中的值最低。电泳时，共分离出六条同工酶带。注意到两个主要的活性区。它们是慢速移动的阳极带（同工酶1、2和3）和快速移动的阴极带（同工酶4、5和6）。脾脏拥有最多的同工酶（带1、2、4、5和6），前列腺有三种（带1、2和3）。心脏只含有一种（带2）。其余器官中发现两种同工酶（带1和2）。抑制剂作用的结果表明，氟化钠抑制所有六种同工酶，而L(+)酒石酸主要抑制阳极区的同工酶。D(-)酒石酸和甲醛对任何同工酶均无明显抑制作用。对氯汞苯甲酸（PCMB）被发现是同工酶3的特异性抑制剂。在宿主去势后，前列腺、肝脏和精囊中酶的活性显著降低。酶活性的这种降低涉及这三个器官中的所有同工酶，但前列腺中的同工酶3在去势后完全消失。这些同工酶的活性通过睾酮替代得以恢复。这些结果表明，大鼠组织中的酸性磷酸酶有多种形式；每种形式在丙烯酰胺凝胶中都有其自身的电泳迁移率、对抑制剂的敏感性以及对激素操纵的反应。同工酶3对前列腺具有特异性，对PCMB抑制和雄激素刺激具有独特的敏感性。
