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Forms and activity of high molecular weight acth in guinea pig

Forms and activity of high molecular weight acth in guinea pig

Peptides 1(3): 223-230

ISSN/ISBN: 0196-9781

High MW forms of ACTH and endorphin were identified in extracts of guinea pig anterior and inermediate/posterior pituitary. Extracts of anterior pituitary contained ACTH immunoactive material with apparent MW of 36,000, 24,000 and 4500 daltons. The highest MW form of ACTH co-migrated with a peak of endorphin immunoactive material. No material the size of glycosylated ACTH(1-39) was detected. Separated forms of high MW ACTH prepared from mouse tumor cell culture medium stimulated the same maximal production of steroid as ACTH(1-39) in the guinea pig adrenal cell bioassay. Pro-ACTH/endorphin and ACTH biosynthetic intermediate were 2 orders of magnitude less potent than synthetic human ACTH(1-39); glycosylated ACTH(1-39) was equipotent to ACTH(1-39) although no similar material was detected in guinea pig pituitary extracts. Isolated guinea pig adrenal cortical cells were incubated with the various separated forms of mouse tumor cell ACTH and products synthesized from (3H)pregnenolone were analyzed by 2-dimensional TLC. The ratio of cortisol-related to corticosterone-related products was the same in response in glycosylated and nonglycosylated ACTH. [Synthetic camet .beta.-endorphin was used as the standard in all endorphin immunoassays.].

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Accession: 005481842

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