期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1981
卷号：78
期号：12
页码：7290-7293
DOI：10.1073/pnas.78.12.7290
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Difference spectra generated during thermolysin digestion of camel beta-endorphin at pH 8.2 or at pH 6.5 indicate rapid blue shifting of the near-UV absorption bands of the NH2-terminal tyrosine. A similar spectral change is not observed for the NH2-terminal tyrosine in [Met]enkephalin when it is digested under similar conditions. These results suggest that enzymatic digestion destroys or alters some structural interaction between the NH2-terminal tyrosyl residue of the endorphin and a residue(s) within the COOH-terminal segment of the molecule. Peptide mapping of the digest as a function of time suggests that cleavage of the bond linking the alanine-21 and isoleucine-22 residues produces most of the observed effect. These data provide evidence for the existence of a tertiary structure for beta-endorphin in aqueous solutions.
