Baxter J H, Suelter C H
Arch Biochem Biophys. 1984 Feb 1;228(2):397-406. doi: 10.1016/0003-9861(84)90003-1.
There are at least three forms of acid phosphatase in avian pectoralis muscle differing in molecular weight, subcellular location, and response to various substrates and inhibitors. These enzymes are separated by differential sedimentation into postmicrosomal supernatant, lysosomal, and microsomal activities with apparent molecular weights in Triton X-100 of 68,000, 198,000, and 365,000, respectively. All of the enzymes show acid pH optima (pH approximately 5), but the postmicrosomal supernatant form is distinctly different from the other two forms in its resistance to most common phosphatase inhibitors and in its reduced activity against several organic phosphates. Quantitation of these three forms of acid phosphatase in normal and dystrophic avian pectoralis muscle shows that the postmicrosomal supernatant form is significantly elevated in dystrophic muscle; at 33 days ex ovo, 84% of the increased acid phosphatase activity in dystrophic muscle can be attributed to the postmicrosomal supernatant form. The microsomal form is only slightly elevated; the level of the lysosomal form is not altered.
禽胸肌中至少存在三种酸性磷酸酶，它们在分子量、亚细胞定位以及对各种底物和抑制剂的反应方面存在差异。这些酶通过差速沉降被分离为微粒体后上清液、溶酶体和微粒体活性，在Triton X-100中的表观分子量分别为68,000、198,000和365,000。所有这些酶的最适pH均为酸性（pH约为5），但微粒体后上清液形式在对大多数常见磷酸酶抑制剂的抗性以及对几种有机磷酸盐的活性降低方面与其他两种形式明显不同。对正常和营养不良的禽胸肌中这三种酸性磷酸酶的定量分析表明，微粒体后上清液形式在营养不良的肌肉中显著升高；在出壳后33天，营养不良肌肉中酸性磷酸酶活性增加的84%可归因于微粒体后上清液形式。微粒体形式仅略有升高；溶酶体形式的水平没有改变。
