Abstract
A BIOLOGICALLY active peptide which is chemically and physiologically distinct from known pituitary hormones has recently been isolated and characterized1. Its purity has been established by various criteria such as column chromatography and gel filtration, zone electrophoresis and disk electrophoresis, countercurrent distribution and sedimentation. This peptide, which was obtained in the course of the isolation of adrenocorticotropin (ACTH) by a revised method2, is more acidic than the latter hormone, and consists of 59 amino-acids. Its molecular weight was determined by sedimentation equilibrium investigations and found to be 6,900. It is structurally different from ACTH, having lysine rather than phenylalanine at the COOH-terminus, and glutamic acid rather than the serine at the NH2-terminus; furthermore, it has a different amino-acid composition. It has a very low adrenocorticotropic activity, and resembles ACTH in melanocyte-stimulating activity; however, it is not potentiated by treatment with boiling NaOH, as is ACTH. Although the lipolytic potencies in the rabbit as determined in vitro were comparable for both peptides, they differed markedly in the rat.
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LI, C. Lipotropin, a New Active Peptide from Pituitary Glands. Nature 201, 924 (1964). https://doi.org/10.1038/201924a0
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DOI: https://doi.org/10.1038/201924a0
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