Franco F J, Diaz C, Barcia M, Freire M
Departamento de Bioquímica e Bioloxía Molecular, Facultade de Bioloxía, Universidade de Santiago de Compostela, Spain.
Biochim Biophys Acta. 1992 Mar 27;1120(1):43-8. doi: 10.1016/0167-4838(92)90422-a.
Failure to detect thymosin alpha 1 (T alpha 1) in tissue extracts prepared by procedures that prevent proteolytic activity has hitherto supported the suggestion that T alpha 1 is not a natural peptide, but the product of uncontrolled proteolysis of prothymosin alpha (ProT alpha), a polypeptide that includes T alpha 1 at its NH2 terminus. In this work, purification by isoelectric focusing of a product with the same isoelectric point as synthetic T alpha 1, and its further characterization, demonstrated that T alpha 1 is present as a native peptide in calf thymus and in several lymphoid and non-lymphoid rat tissues. T alpha 1 shows abnormal chromatographic behaviour which appears to be due to association with other components in tissue extracts. In all the tissues studied, T alpha 1 was present in higher concentration than ProT alpha (80-183 and 44-123 micrograms per gram of tissue, respectively). The ProT alpha/T alpha 1 ratio did not change when no measures were taken to prevent proteolysis during tissue homogenization.
通过防止蛋白水解活性的方法制备的组织提取物中未能检测到胸腺素α1(Tα1),这一直支持了这样一种观点,即Tα1不是天然肽,而是前胸腺素α(ProTα)不受控制的蛋白水解产物,ProTα是一种在其NH2末端包含Tα1的多肽。在这项工作中,通过等电聚焦对一种与合成Tα1具有相同等电点的产物进行纯化,并对其进一步表征,结果表明Tα1以天然肽的形式存在于小牛胸腺以及几种大鼠淋巴和非淋巴组织中。Tα1表现出异常的色谱行为,这似乎是由于与组织提取物中的其他成分相关联所致。在所有研究的组织中,Tα1的浓度均高于ProTα(分别为每克组织80 - 183微克和44 - 123微克)。当在组织匀浆过程中未采取措施防止蛋白水解时,ProTα/Tα1的比值没有变化。