Processing of adrenocorticotropin by two proteases in bovine intermediate lobe secretory vesicle membranes. A distinct acidic, tetrabasic residue-specific calcium-activated serine protease and a PC2-like enzyme

Adrenocorticotropin (ACTH) is cleaved at the tetrabasic residue site, in pituitary intermediate lobe secretory vesicles, to yield ACTH1-17 and corticotropin-like intermediate lobe peptide (CLIP). ACTH1-17 is then converted to alpha-melanocyte-stimulating hormone (N-AcACTH1-13NH2) by first removing t...

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Veröffentlicht in:	The Journal of biological chemistry 1992-04, Vol.267 (11), p.7456-7463
Hauptverfasser:	ESTIVARIZ, F. E, FRIEDMAN, T. C, CHIKUMA, T, LOH, Y. P
Format:	Artikel
Sprache:	eng
Schlagworte:	Adrenocorticotropic Hormone - metabolism alpha-MSH - metabolism Amino Acid Sequence Aminoacids, peptides. Hormones. Neuropeptides Analytical, structural and metabolic biochemistry Animals Aspartic Acid Endopeptidases - antagonists & inhibitors Biological and medical sciences Calcium - metabolism Cattle Chromatography, High Pressure Liquid Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Hydrolysis Molecular Sequence Data Peptide Fragments - metabolism Pituitary Gland - metabolism Protein Processing, Post-Translational Proteins Serine Endopeptidases - metabolism Serine Proteinase Inhibitors - pharmacology
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