Glämsta E L, Nyberg F, Silberring J
Department of Pharmacology, University of Uppsala, Sweden.
Rapid Commun Mass Spectrom. 1992 Dec;6(12):777-80. doi: 10.1002/rcm.1290061213.
Recent studies have revealed the presence of a new group of opioid peptides, the hemorphins, in the human pituitary as well as in human cerebrospinal fluid. The hemorphins are structurally related to sequence segments residing in the beta, delta, gamma or epsilon-chains of hemoglobin. In this study we have applied fast-atom bombardment mass spectrometry (FAB-MS) to elucidate the sequence of a hemorphin fragment isolated from the cerebrospinal fluid of patients with cerebrovascular bleedings. The FAB-MS was used in conjunction with carboxypeptidase Y digestion and results indicated that this procedure proved to be a powerful tool for rapid sequence determination. The recovered peptide was thus found to be identical with the sequence 32-41 of the above mentioned hemoglobin chains.
最近的研究表明,在人类垂体以及人类脑脊液中存在一组新的阿片肽——血啡肽。血啡肽在结构上与血红蛋白β、δ、γ或ε链中的序列片段相关。在本研究中,我们应用快原子轰击质谱法(FAB-MS)来阐明从脑血管出血患者脑脊液中分离出的血啡肽片段的序列。FAB-MS与羧肽酶Y消化法结合使用,结果表明该方法是快速序列测定的有力工具。因此发现回收的肽与上述血红蛋白链的32-41序列相同。