TY - JOUR
T1 - Sheep testicular and epididymal angiotensin converting enzyme
T2 - Inhibitions by captopril, lisinopril and enalapril
AU - Udupa, E. G P
AU - Rao, N. Mallikarjuna
PY - 1997/12/23
Y1 - 1997/12/23
N2 - Inhibition of angiotensin converting enzyme (ACE) in presence of captopril (C), lisinopril (L) and enalapril (E) were investigated in testis and epididymis of sheep using Hip-His-Leu as substrate. Captopril, lisinopril and enalapril were competitive inhibitors of the enzyme from both tissues. Differences in the I50 and K(i) values using these three inhibitors reflects the affinities of these inhibitors for the ACE. In addition, the relative potencies of captopril, lisinopril and enalapril were different for testicular ACE (C > L > E) and epididymal ACE (L > C > E). This observation suggests differences between the active sites of the testicular and epididymal ACE which may reflect on their functions in vivo.
AB - Inhibition of angiotensin converting enzyme (ACE) in presence of captopril (C), lisinopril (L) and enalapril (E) were investigated in testis and epididymis of sheep using Hip-His-Leu as substrate. Captopril, lisinopril and enalapril were competitive inhibitors of the enzyme from both tissues. Differences in the I50 and K(i) values using these three inhibitors reflects the affinities of these inhibitors for the ACE. In addition, the relative potencies of captopril, lisinopril and enalapril were different for testicular ACE (C > L > E) and epididymal ACE (L > C > E). This observation suggests differences between the active sites of the testicular and epididymal ACE which may reflect on their functions in vivo.
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U2 - 10.1080/15216549700204881
DO - 10.1080/15216549700204881
M3 - Article
C2 - 9415815
AN - SCOPUS:0030862254
SN - 1039-9712
VL - 43
SP - 1063
EP - 1070
JO - Biochemistry and Molecular Biology International
JF - Biochemistry and Molecular Biology International
IS - 5
ER -