Abstract
Some analogues of bradykinin, especially with replacements by other amino acids of phenylalanine in position 8, have been investigated for enzymatic stability against kininase II from rat duodenum microsomes and rat uterus plasma membranes, respectively. As compared with bradykinin, two of the analogues, [8-erythro-beta-phenylserine]- and [8-erythro-alpha-Amino-beta-phenylbutyric acid]-Bradykinin were stable to enzymatic degradation. Therefore, the latter may be used for studies in hormone-receptor interaction.
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