Molecular cloning and response to laminarin stimulation of arginine kinase in haemolymph in Chinese shrimp, Fenneropenaeus chinensis.
Molecular cloning and response to laminarin stimulation of arginine kinase in haemolymph in Chinese shrimp, Fenneropenaeus chinensis.
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DOI：
10.1016/j.fsi.2005.01.006
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发表时间：
2005-10
影响因子：
4.7
通讯作者：
C. Yao;Changgong Wu;J. Xiang;Bo Dong
中科院分区：
文献类型：
--
作者：
C. Yao;Changgong Wu;J. Xiang;Bo Dong
精氨酸激酶（AK）以前被报道为无脊椎动物中发现的磷酸酶-ATP磷酸转移酶。本研究克隆了一个1184 bp的cDNA序列。该基因包含一个1068 bp的开放阅读框架，编码中国明对虾AK蛋白的356个氨基酸。AK的计算分子量为40129.73 Da，pI为5.92。预测的蛋白质显示出高水平的身份，已知AK在无脊椎动物和肌酸激酶从脊椎动物，属于一个保守的家庭的ATP：胍磷酸转移酶。此外，F.根据计算的分子量和pI值，采用双向电泳（2DE）和电喷雾质谱（ESI-MS）技术对其中一种进行了鉴定。F. 2DE和ESI-MS结果表明，注射海带多糖后45 min，中国对虾血浆蛋白中AK蛋白含量显著下降，注射海带多糖后3 h，AK蛋白含量恢复正常。在模拟后45 min和3 h，
Arginine kinase (AK) was previously reported as a phosphagen-ATP phosphotransferase found in invertebrates. In this study, an 1184 bp cDNA was cloned and sequenced. It contained an open reading frame of 1068 bp that coded for 356 deduced amino acids of AK in Fenneropenaeus chinensis. The calculated molecular mass of AK is 40129.73 Da and pI is 5.92. The predicted protein showed a high level of identity to known AK in invertebrates and creatine kinase from vertebrates, which belong to a conserved family of ATP:guanidino phospho-transferases. In addition, AK protein in plasma of F. chinensis was identified using two-dimensional electrophoresis (2DE) and electrospray ionization mass spectrometry (ESI-MS) according to the calculated molecular mass and pI. AK was significantly decreased in the plasma of F. chinensis at 45 min and recovered at 3 h after laminarin injection as confirmed by 2DE and ESI-MS. The results showed that AK was one of the most significantly changed proteins on two-dimensional gel in the plasma proteins of F. chinensis at 45 min and 3 h after simulation.