Application of fast-atom bombardment mass spectrometry for sequencing of a hemoglobin fragment, naturally occurring in human cerebrospinal fluid.
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.
Glämsta
E L
EL
Department of Pharmacology, University of Uppsala, Sweden.
Nyberg
F
F
Silberring
J
J
D000595:Amino Acid Sequence; D002268:Carboxypeptidases; D002851:Chromatography, High Pressure Liquid; D006454:Hemoglobins / Q000134:cerebrospinal fluid*; D006801:Humans; D006868:Hydrolysis; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000134:cerebrospinal fluid*; D016339:Spectrometry, Mass, Fast Atom Bombardment
D006454:Hemoglobins; D010446:Peptide Fragments; D002268:Carboxypeptidases; C022633:serine carboxypeptidase