Angiotensin-converting enzyme C-terminal catalytic domain is the main site of angiotensin I cleavage in vivo

Hypertension

Volumn 51, Issue 2, 2008, Pages 267-274

  Fuchs, Sebastien ^a,e   Xiao, Hong D ^a   Hubert, Christine ^b   Michaud, Annie ^b   Campbell, Duncan J ^c   Adams, Jonathan W ^a   Capecchi, Mario R ^d   Corvol, Pierre ^b   Bernstein, Kenneth E ^a  

^a EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b INSERM   (France)

^c UNIVERSITY OF MELBOURNE   (Australia)

^d UNIVERSITY OF UTAH SCHOOL OF MEDICINE   (United States)

^e EMORY UNIVERSITY   (United States)

Author keywords

Angiotensin; Angiotensin converting enzyme; Blood pressure; Bradykinin; Catalytic sites; Genetic mice model; Male infertility

Indexed keywords

ANGIOTENSIN I; BRADYKININ; CHLORIDE; DIPEPTIDYL CARBOXYPEPTIDASE; RENIN; ZINC;

ANIMAL EXPERIMENT; ARTICLE; BLOOD PRESSURE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONTROLLED STUDY; DEHYDRATION; ENZYME ACTIVITY; GENE TARGETING; HYDROLYSIS; KIDNEY; MOUSE; NONHUMAN; PLASMA RENIN ACTIVITY; POINT MUTATION; PRIORITY JOURNAL; PROTEIN BLOOD LEVEL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN MOTIF; WILD TYPE;

ANGIOTENSIN I; ANGIOTENSIN II; ANGIOTENSINS; ANIMALS; BLOOD PRESSURE; BRADYKININ; CATALYTIC DOMAIN; HEMATOCRIT; INFUSIONS, INTRAVENOUS; KIDNEY; MICE; MICE, MUTANT STRAINS; OSMOLAR CONCENTRATION; PEPTIDYL-DIPEPTIDASE A; POINT MUTATION; RENIN; SUBSTRATE SPECIFICITY; ZINC FINGERS;

EID: 38549119426     PISSN: 0194911X     EISSN: None     Source Type: Journal    
DOI: 10.1161/HYPERTENSIONAHA.107.097865     Document Type: Article

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