{'fraction_non_alphanumeric': 0.055345911949685536, 'fraction_numerical': 0.033962264150943396, 'mean_word_length': 5.21875, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Evidence for the Internalization of [125I‐TYR2, NLE4, D‐PHE7] α‐MSH following Binding to the MSH Receptor of B16 Murine Melanoma Cells

The mechanism of action of a-melanocyte stimulating hormone (a-MSH) is thought to be receptor-mediated induction of CAMP, which in turn produces an increase in tyrosinase and melanin content. a-MSH is a 13 amino acid peptide that binds to melanoma cells. Previous studies have suggested that binding occurs at the cell surface without internalization,’ In this study, the internalization of [‘251-Tyr2,Nle4,~-Phe7]a-MSH following binding by B 16 mouse melanoma cells has been investigated. The amount of peptide internalized was differentiated from surface-bound ligand by acid dissociation (pH 2.5) of surface-bound radiolabeled [1251-Tyr2,Nle4,~-Phe7]~-MSH.