Kunze D, Rüstow B, Olthoff D, Jung K
Clin Chim Acta. 1985 Mar 15;146(2-3):167-74. doi: 10.1016/0009-8981(85)90055-5.
Biopsy samples from normal and dystrophic human muscle (Duchenne type) were fractionated by differential centrifugation and microsomes, mitochondria and cytosol were assayed for phosphatidic acid phosphatase (EC 3.1.3.4) and marker enzymes of mitochondria and cytosol. The activity of phosphatidic acid phosphatase was significantly lower in microsomes and higher in cytosol and mitochondria of dystrophic muscle than in the corresponding subcellular fractions of normal muscle. The results support an explanation of earlier findings that there is reduced G3P incorporation into diglycerides and phosphatidylcholine and a qualitative and quantitative change in the amount of phosphatidylcholine in dystrophic microsomes. The possible reasons for the reduction in the activity of only microsomal PA-P-ase were discussed.
从正常和营养不良的人类肌肉(杜兴氏型)中获取活检样本,通过差速离心法进行分级分离,然后检测微粒体、线粒体和胞质溶胶中的磷脂酸磷酸酶(EC 3.1.3.4)以及线粒体和胞质溶胶的标记酶。与正常肌肉相应的亚细胞组分相比,营养不良肌肉的微粒体中磷脂酸磷酸酶的活性显著降低,而胞质溶胶和线粒体中的活性则更高。这些结果支持了对早期发现的一种解释,即甘油-3-磷酸掺入甘油二酯和磷脂酰胆碱的过程减少,并且营养不良微粒体中磷脂酰胆碱的数量在质量和数量上都发生了变化。文中讨论了仅微粒体PA-P-ase活性降低的可能原因。