Galoyan A A, Abrahamian G E, Chailyan S G, Hashim G A, Lajtha A
Department of Neurohormone Biochemistry, Academy of Sciences of Armenia, Yerevan.
Neurochem Res. 1994 Apr;19(4):451-6. doi: 10.1007/BF00967323.
A fragment (11-19) of thymosin beta 4 was found to stimulate phosphodiesterase activity even in the absence of calcium and calmodulin. Half-maximal enzyme activation occurred with 10 nM peptide, and was further increased by phospholipids such as phosphatidylserine. The mechanism of stimulation is an increase in the Vmax of cAMP degradation without a substantial change in the Km for the substrate. In the presence of calcium ions and calmodulin the peptide was also stimulatory.
胸腺素β4的一个片段(11 - 19)被发现即使在没有钙和钙调蛋白的情况下也能刺激磷酸二酯酶活性。10 nM的肽可使酶激活达到半数最大效应,并且磷脂如磷脂酰丝氨酸可进一步增强这种激活作用。刺激机制是cAMP降解的Vmax增加,而底物的Km没有实质性变化。在钙离子和钙调蛋白存在的情况下,该肽也具有刺激作用。