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Purification and Characterisation of Cerebellins from Human and Porcine Cerebellum
Author(s) -
Yiangou Y.,
Burnet P.,
Nikou G.,
Chrysanthou B. J.,
Bloom S. R.
Publication year - 1989
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1989.tb11787.x
Subject(s) - edman degradation , peptide , radioimmunoassay , molecular mass , peptide sequence , mass spectrometry , chemistry , biochemistry , biology , sequence (biology) , protein primary structure , chromatography , gene , enzyme
The primary human and porcine structure of the novel neuropeptide cerebellin is unknown. These peptides were, therefore, isolated by a combination of ion‐exchange and reverse‐phase chromatography using a specific radioimmunoassay against rat cerebellin. The sequences of the peptides were deduced by mass spectrometry (for both human and porcine cerebellins) and gas‐phase Edman degradation (for porcine cerebellin). In both species, two molecular forms were identified. In the human, the major form corresponded to the pentadecamer [des‐Ser 1 ]‐cerebellin (˜95% of the total) and the minor form, to the hexadecamer peptide. In the pig. however, both molecular forms were present in approximately equal amounts. The finding that the sequences of human and porcine cerebellin are identical to that of the rat suggests that strong evolutionary pressure has acted to conserve this sequence.