Elmore M A, Griffiths E C, O'Connor B, O'Cuinn G
Department of Biochemistry, University College, Galway, Ireland.
Neuropeptides. 1990 Jan;15(1):31-6. doi: 10.1016/0143-4179(90)90157-t.
In this study the substrate specificity of a pyroglutamate aminopeptidase from synaptosomal membranes of guinea-pig brain was investigated. The enzyme was found to be specific for tripeptides, tripeptide-amides and tetrapeptides which possess the N-terminal sequence Glp-His and as such is specific for Thyrotropin Releasing Hormone or only very closely related peptides. The enzyme was found not to hydrolyse a number of analogues of Thyrotropin Releasing Hormone which have been shown to have therapeutical value in certain neuronal disorders.
在本研究中，对来自豚鼠脑突触体膜的焦谷氨酸氨肽酶的底物特异性进行了研究。发现该酶对具有N端序列谷氨酰胺-组氨酸的三肽、三肽酰胺和四肽具有特异性，因此对促甲状腺激素释放激素或仅与其密切相关的肽具有特异性。还发现该酶不能水解促甲状腺激素释放激素的一些类似物，而这些类似物已被证明在某些神经元疾病中具有治疗价值。
