Khan N A, Masson I, Quemener V, Clari G, Moret V, Moulinoux J P
Unité Fonctionnelle de Biologie Cellulaire CNRS SDI, Centre Hospitalier Universitaire, Rennes, France.
Biochem Int. 1990;20(5):863-8.
In vitro regulation of cytosolic tyrosine protein (Tyr-P) kinase from human erythrocytes by polyamines, polyamino acids, negative charged compounds or by insulin using angiotensin II or poly (Glu-Tyr)4:1 as substrates was studied. All the three polyamines, putrescine (Put), spermidine (Spd) and spermine (Spm) stimulated the Tyr-P kinase activity in a dose dependent manner. Spm stimulated Tyr-P kinase activity higher than Put and Spd whether the substrate was angiotension II or poly (Glu-Tyr)4:1. Polyamino acids (polyornithine, polyarginine, polyglutamic acid and polyaspartic acid) did not affect significantly the Tyr-P kinase phosphorylation except polylysine which significantly stimulated the Tyr-P kinase activity. Negative charged compounds (chondroitin sulfate A, B and C) and heparin inhibited the Tyr-P kinase phosphorylation while insulin did not influence the enzyme activity in the presence of either substrates.
研究了多胺、多氨基酸、带负电荷化合物或胰岛素以血管紧张素 II 或聚（谷氨酰胺 - 酪氨酸）4:1 为底物对人红细胞胞质酪氨酸蛋白（Tyr - P）激酶的体外调节作用。三种多胺，即腐胺（Put）、亚精胺（Spd）和精胺（Spm），均以剂量依赖方式刺激 Tyr - P 激酶活性。无论底物是血管紧张素 II 还是聚（谷氨酰胺 - 酪氨酸）4:1，Spm 刺激 Tyr - P 激酶活性的程度均高于 Put 和 Spd。多氨基酸（聚鸟氨酸、聚精氨酸、聚谷氨酸和聚天冬氨酸）对 Tyr - P 激酶磷酸化作用影响不显著，只有聚赖氨酸能显著刺激 Tyr - P 激酶活性。带负电荷的化合物（硫酸软骨素 A、B 和 C）以及肝素抑制 Tyr - P 激酶磷酸化，而在存在任何一种底物的情况下，胰岛素均不影响该酶活性。
