Hydrolysis of neo-kyotorphin (Thr-Ser-Lys-Tyr-Arg) and [Met]enkephalin-Arg6-Phe7 by angiotensin-converting enzyme from monkey brain
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Cited by (21)
The angiotensin converting enzyme (ACE) inhibitor, captopril disrupts the motility activation of sperm from the silkworm, Bombyx mori
2017, Journal of Insect PhysiologyCitation Excerpt :This cleavage can contribute to hypertension by promoting vascular smooth muscle vasoconstriction and renal tubule sodium reabsorption; hence this enzyme is generally known as angiotensin-converting enzyme (ACE) (Corvol et al., 2004). On the other hand, ACE is also known as a relatively nonspecific peptidase that can hydrolyze a wide range of small peptides in vitro (Skidgel et al., 1984; Skidgel and Erdös, 1985; Kase et al., 1986; Dubreuil et al., 1989). At present, in vivo ACE activity has already been shown to play roles in many different physiological processes in several different tissues, including the lungs, small intestine, choroid plexus and lymphocytes (Azizi et al., 1996, 1997).
Expression of angiotensin-converting enzyme-related carboxydipeptidases in the larvae of four species of fly
1997, Insect Biochemistry and Molecular BiologyKinetic evaluation of β-neoendorphin hydrolysis by the somatic and testicular isozymes of human angiotensin-converting enzyme
1997, Biochimica et Biophysica Acta - Protein Structure and Molecular EnzymologyLocalization of angiotensin converting enzyme by in vitro autoradiography in the rabbit brain
1995, Journal of Chemical NeuroanatomyIsolation and identification of an endogenous inhibitor of enkephalin-degrading enzymes from bovine spinal cord
1993, Biochemical and Biophysical Research Communications
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