Abstract
The molecular forms of proopiomelanocortin (POMC) derived amidated and C-terminal glycine-extended joining peptide from monkey (Macaca mulatta) pituitary were determined. The predominant forms of joining peptide found were the low molecular peptides POMC(76-105) and POMC(76-106), respectively. Significant amounts of N-terminally truncated POMC(78-105) and POMC(78-106) were also detected in the posterior-intermediate lobe. No N-terminal extended forms were detected. The relative amount of amidated joining peptide to total joining peptide was 6-35%. It is concluded that not only is the primary sequence of monkey and human POMC extremely conserved, but also the processing patterns are similar. The monkey therefore serves as a suitable model for studying regulation of the processing of POMC and the hypothalamus-pituitary-adrenal axis in man.
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