Sarcoplasmic reticulum. VII. Properties of a phosphoprotein intermediate implicated in calcium transport.
Sarcoplasmic reticulum. VII. Properties of a phosphoprotein intermediate implicated in calcium transport.
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肌浆网。
DOI：
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发表时间：
1969
影响因子：
4.8
通讯作者：
A. Martonosi
中科院分区：
文献类型：
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作者：
A. Martonosi
骨骼肌微粒体水解32 P标记的三磷酸腺苷是通过蛋白质结合的磷酸中间体进行的。中间体的稳态浓度受孵育介质的离子环境、温度和pH值的影响。用磷脂酶C处理微粒体导致ATP酶活性和Ca++转运的抑制，磷酸化中间体的浓度增加。用合成卵磷脂恢复ATP酶活性和Ca++转运伴随着磷酸化中间体浓度的下降。羟胺抑制ATP酶活性、Ca ~（++）转运和磷酸化中间体的形成。基于其pH稳定性和对羟胺的敏感性，磷酸化中间体可能是酰基磷酸。通过高压电泳从胃蛋白酶消化的32 P标记的微粒体中分离32 P标记的肽。
Abstract Hydrolysis of 32P-labeled adenosine triphosphate by skeletal muscle microsomes occurs through a protein-bound phosphate intermediate. The steady state concentration of intermediate is influenced by the ionic milieu, temperature, and pH of the incubation medium. Treatment of microsomes with phospholipase C causes the inhibition of ATPase activity and Ca++ transport, with an increase in the concentration of phosphorylated intermediate. Restoration of ATPase activity and Ca++ transport with synthetic lecithin is accompanied by a decline of the phosphorylated intermediate concentration. Hydroxylamine inhibits the ATPase activity, Ca++ transport, and formation of phosphorylated intermediate in similar concentration. On the basis of its pH stability and sensitivity to hydroxylamine the phosphorylated intermediate is probably an acyl phosphate. A 32P-labeled peptide was separated by high voltage electrophoresis from a pepsin digest of 32P-labeled microsomes.