Pfeifle J, Anderer F A
Biochim Biophys Acta. 1983 Feb 16;762(1):86-93. doi: 10.1016/0167-4889(83)90120-9.
Investigation of the cellular distribution of a 105 kDa phosphoprotein (pp 105) in transformed mouse fibroblasts, showed that only a minor amount was located on the surface of logarithmically grown suspension cells. More than 90% of total pp 105 was contained in the cytosolic fraction representing about 0.2% of total cytosolic proteins. Surface and cytosolic pp 105 had identical phosphopeptide patterns. Cytosolic pp 105 was highly purified by ammonium sulfate precipitation followed by three chromatographic steps and gel electrophoresis. The purified pp 105 was capable of weak autophosphorylation. In the stationary growth phase of suspension cells, the amount of pp 105 detectable by endogenous phosphorylation was only 10-15% of that observed during logarithmic growth. pp 105 was also detected in normal mouse tissue and its distribution determined.
对转化的小鼠成纤维细胞中一种105 kDa磷蛋白（pp 105）的细胞分布进行研究，结果表明，对数生长期悬浮细胞表面仅存在少量该蛋白。pp 105总量的90%以上存在于胞质组分中，约占胞质总蛋白的0.2%。表面和胞质中的pp 105具有相同的磷酸肽图谱。通过硫酸铵沉淀，随后经过三步色谱法和凝胶电泳，对胞质中的pp 105进行了高度纯化。纯化后的pp 105能够进行微弱的自身磷酸化。在悬浮细胞的静止生长期，通过内源性磷酸化可检测到的pp 105量仅为对数生长期所观察到量的10 - 15%。在正常小鼠组织中也检测到了pp 105，并确定了其分布。
