Purification and characterization of high-molecular-weight forms of adrenocorticotropic hormone of ovine pituitary glands

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Abstract
A highly purified preparation of high MW ACTH was prepared from ovine pituitary glands by dilute acetic acid extraction, oxycellulose fractionation, Sephadex gel filtration and affinity chromatography on immobilized .alpha.p(1-39)ACTH antibodies. Two ACTH peptides of MW of 24,000 and 34,000 were detected by sodium dodecyl sulfate-acrylamide gel electrophoresis in this preparation. The immobilized antibodies apparently adsorbed 2 forms equally well and could not distinguish between them under the conditions used. These 2 ACTH peptides were present in crude extracts of ovine pituitary glands, indicating that they were not artifacts produced by the purification procedure. The high MW forms of ACTH were susceptible to degradation by tissue enzymes. They could be easily destroyed during the extraction, if precautions were not taken. They were poorly adsorbed by oxycellulose which had been used for the adsorption of ACTH activity from crude preparations by most investigators. These properties probably accounted for the fact that high MW forms of ACTH remained undetected until very recently. [Human serum albumin, porcine pepsin, bovine RNase, rabbit aldolase and pigeon crop sac were used.].

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