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Journal of Endocrinology (1974) 61, 369-380       DOI: 10.1677/joe.0.0610369
© 1974 Society for Endocrinology
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PURIFICATION AND CHARACTERIZATION OF PORCINE CORTICOTROPHIN-LIKE INTERMEDIATE LOBE PEPTIDE

A. P. SCOTT, P. J. LOWRY, H. P. J. BENNETT, C. McMARTIN and J. G. RATCLIFFE

Pig posterior pituitary lobe powder contains a peptide structurally identical to the 18–39 portion of porcine adrenocorticotrophin (ACTH). Its extraction by several different procedures is described and its susceptibility to degradation in the presence of 5% acetic acid has been noted. This degradation has been ascribed to the presence of acid proteases in the acetone-dried powder of the posterior pituitary lobe. The peptide has been isolated by chromatography on Biogel P6 and DEAE-cellulose, and characterized by enzyme fragmentation studies. It resembles the peptide isolated from rat neurointermediate lobes termed 'corticotrophin-like intermediate lobe peptide' and it is suggested that it is derived by the intracellular cleavage of ACTH in the pars intermedia cells, with subsequent formation of {alpha}-melanocyte-stimulating hormone from the other adrenocorticotrophic fragment.







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