Abstract
Pyroglutamylhistidylproline and histidylproline, reported metabolites of thyrotropin releasing hormone, were found to competitively inhibit purified rabbit lung angiotensin converting enzyme with K I values of 0.76 μM and 1.7 mM, respectively. Native thyrotropin releasing hormone and histidylprolinediketopiperazine at concentrations of 10 mM and 5 mM, respectively, had no effect on angiotensin converting enzyme activity. Neither the native hormone nor its deamidated derivative served as substrate for angiotensin converting enzyme.
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