Purification and characterisation of cerebellins from human and porcine cerebellum.
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-Ser1]-cerebellin (approximately 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.
Yiangou
Y
Y
Department of Medicine, Royal Postgraduate Medical School, Hammersmith Hospital, London, England, U.K.
Burnet
P
P
Nikou
G
G
Chrysanthou
B J
BJ
Bloom
S R
SR
D000595:Amino Acid Sequence; D000818:Animals; D002531:Cerebellum / Q000032:analysis*; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D006801:Humans; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009419:Nerve Tissue Proteins / Q000302:isolation & purification*; D011863:Radioimmunoassay; D013552:Swine
D009419:Nerve Tissue Proteins; C046788:cerebellin