PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19629962-2 2010 A rapid and sensitive analysis method or ACE activity by quantifying simultaneously the substrate hippuryl-histidyl-leucine and its product hippuric acid using an ultra-performance liquid chromatography coupled with electrospray ionization-mass spectrometry (UPLC-MS) was first developed and applied to assay the inhibitory activities against ACE of several natural phenolic compounds. hippuryl-histidyl-leucine 98-123 angiotensin I converting enzyme Homo sapiens 41-44 19629962-2 2010 A rapid and sensitive analysis method or ACE activity by quantifying simultaneously the substrate hippuryl-histidyl-leucine and its product hippuric acid using an ultra-performance liquid chromatography coupled with electrospray ionization-mass spectrometry (UPLC-MS) was first developed and applied to assay the inhibitory activities against ACE of several natural phenolic compounds. hippuryl-histidyl-leucine 98-123 angiotensin I converting enzyme Homo sapiens 343-346 19149231-4 2008 The serum and tissue ACE activity was determined before and after therapy, using the spectrophotometric method and hippuryl-l-histidyl-l-leucine as a substrate. hippuryl-histidyl-leucine 115-144 angiotensin I converting enzyme Homo sapiens 21-24 19839596-2 2009 A colorimetric assay to measure hippuric acid (HA) was transformed into a rapid ACE assay wherein the released HA from the substrate hippuryl-histidyl-leucine (HHL) is mixed with pyridine and benzene sulfonyl chloride. hippuryl-histidyl-leucine 133-158 angiotensin I converting enzyme Homo sapiens 80-83 17386920-2 2007 Most of these have used hippuryl-histidyl-leucine (HHL) as a substrate for ACE reaction with considerable interferences. hippuryl-histidyl-leucine 24-49 angiotensin I converting enzyme Homo sapiens 75-78 17489742-3 2007 The tissue ACE activity was determined before and after therapy, by the spectrophotometric method using hippuryl-l-histidyl-l-leucine as a substrate. hippuryl-histidyl-leucine 104-133 angiotensin I converting enzyme Homo sapiens 11-14 10856278-6 2000 Two peaks (P1 and P2 for premature infants; TP1 and TP2 for full-term infants) with ACE activity on hippuryl-His-Leu (K(m), 3 mmol/L) were detected. hippuryl-histidyl-leucine 100-116 angiotensin I converting enzyme Homo sapiens 84-87 17489765-3 2007 Serum and tissue ACE activity was determined by spectrophotometric method using hippuryl-l-histidyl-l-leucine (Hip-His-Leu) as a substrate. hippuryl-histidyl-leucine 80-109 angiotensin I converting enzyme Homo sapiens 17-20 17489765-3 2007 Serum and tissue ACE activity was determined by spectrophotometric method using hippuryl-l-histidyl-l-leucine (Hip-His-Leu) as a substrate. hippuryl-histidyl-leucine 111-122 angiotensin I converting enzyme Homo sapiens 17-20 16351584-2 2005 Serum and tissue ACE activity was determined by spectrophotometric method using hippuryl-l-histidyl-l-leucine as a substrate. hippuryl-histidyl-leucine 80-109 angiotensin I converting enzyme Homo sapiens 17-20 15526584-3 2004 The serum ACE activity was determined before and after therapy, by the spectrophotometric method using hippuryl-l-histidyl-l-leucine as a substrate. hippuryl-histidyl-leucine 103-132 angiotensin I converting enzyme Homo sapiens 10-13 11975696-3 2002 Serum ACE inhibition profiles were determined in each case using a synthetic substrate, hippuryl-histidyl-leucine (HHL). hippuryl-histidyl-leucine 88-113 angiotensin I converting enzyme Homo sapiens 6-9 10856268-2 2000 The in vitro and in vivo inhibitory potency of omapatrilat and the specific ACE inhibitor fosinopril toward the 2 active sites of ACE (called N- and C-domains) was investigated with the use of 3 substrates: angiotensin I, which is equally cleaved by the 2 ACE domains; hippuryl-histidyl-leucine, specific synthetic substrate of the C-domain in high- salt conditions; and a newly synthesized specific substrate of the N-domain designed by acetylating the lysine residue of AcSDKP. hippuryl-histidyl-leucine 269-294 angiotensin I converting enzyme Homo sapiens 130-133 10856268-2 2000 The in vitro and in vivo inhibitory potency of omapatrilat and the specific ACE inhibitor fosinopril toward the 2 active sites of ACE (called N- and C-domains) was investigated with the use of 3 substrates: angiotensin I, which is equally cleaved by the 2 ACE domains; hippuryl-histidyl-leucine, specific synthetic substrate of the C-domain in high- salt conditions; and a newly synthesized specific substrate of the N-domain designed by acetylating the lysine residue of AcSDKP. hippuryl-histidyl-leucine 269-294 angiotensin I converting enzyme Homo sapiens 130-133 16513436-2 2006 The most commonly used substrate hippuryl-histidyl-leucine (HHL) or hippuryl-glycyl-glycine (HGG) hydrolysis catalyzed by purified rabbit lung ACE or human plasma ACE was investigated in the presence of benazeprilat. hippuryl-histidyl-leucine 33-58 angiotensin I converting enzyme Homo sapiens 163-166 10826406-2 2000 ACE activity in homogenates of T-lymphocytes or in intact T-lymphocytes in suspension was measured by determining fluorimetrically histidyl-leucine, formed from the conversion of hippuryl-histidyl-leucine, coupled with ophtaldialdehyde. hippuryl-histidyl-leucine 179-204 angiotensin I converting enzyme Homo sapiens 0-3 10209009-7 1999 This effect was not due to the inhibition of bradykinin degradation, because no effect was seen in the presence of an inhibitory concentration of the synthetic ACE substrate hippuryl-L-histidyl-L-leucine. hippuryl-histidyl-leucine 174-203 angiotensin I converting enzyme Homo sapiens 160-163 10790312-2 2000 Hippuryl-l-histidyl-l-leucine, a synthetic tripeptide, was used as the ACE-specific substrate. hippuryl-histidyl-leucine 0-29 angiotensin I converting enzyme Homo sapiens 71-74 10323266-3 1999 We found that whole-cell homogenates of both basal (serum-untreated) and squamous-differentiated bronchial epithelial cells degraded hippuryl-L-histidyl-L-leucine, a synthetic substrate for angiotensin-converting enzyme. hippuryl-histidyl-leucine 133-162 angiotensin I converting enzyme Homo sapiens 190-219 1320881-4 1992 When the same peptides were assayed as potential inhibitors of the hydrolysis of hippuryl-His-Leu (specific substrate for ACE activity), substance P and its (1-9) fragment were equally potent, whereas neurokinin A was inactive. hippuryl-histidyl-leucine 81-97 angiotensin I converting enzyme Homo sapiens 122-125 7955411-0 1994 Optimized determination of angiotensin I-converting enzyme activity with hippuryl-L-histidyl-L-leucine as substrate. hippuryl-histidyl-leucine 73-102 angiotensin I converting enzyme Homo sapiens 27-58 8652101-0 1996 Hippuryl-L-histidyl-L-leucine, a substrate for angiotensin converting enzyme. hippuryl-histidyl-leucine 0-29 angiotensin I converting enzyme Homo sapiens 47-76 8883029-3 1996 The activity of angiotensin-converting enzyme was determined by a spectrophotometric method using hippuryl-l-histidyl-l-leucine as a substrate. hippuryl-histidyl-leucine 98-127 angiotensin I converting enzyme Homo sapiens 16-45 7581746-1 1994 We compared angiotensin I-converting enzyme (ACE) and carboxypeptidase A (CPA), two zinc metallopeptidases, for the hydrolysis of the usual ACE synthetic substrate benzoylglycyl-histidyl-leucine (HHL) investigating the possible interference by CPA in the determination of ACE activity in biological fluids. hippuryl-histidyl-leucine 164-194 angiotensin I converting enzyme Homo sapiens 12-43 7581746-1 1994 We compared angiotensin I-converting enzyme (ACE) and carboxypeptidase A (CPA), two zinc metallopeptidases, for the hydrolysis of the usual ACE synthetic substrate benzoylglycyl-histidyl-leucine (HHL) investigating the possible interference by CPA in the determination of ACE activity in biological fluids. hippuryl-histidyl-leucine 164-194 angiotensin I converting enzyme Homo sapiens 45-48 7581746-1 1994 We compared angiotensin I-converting enzyme (ACE) and carboxypeptidase A (CPA), two zinc metallopeptidases, for the hydrolysis of the usual ACE synthetic substrate benzoylglycyl-histidyl-leucine (HHL) investigating the possible interference by CPA in the determination of ACE activity in biological fluids. hippuryl-histidyl-leucine 164-194 angiotensin I converting enzyme Homo sapiens 140-143 7581746-1 1994 We compared angiotensin I-converting enzyme (ACE) and carboxypeptidase A (CPA), two zinc metallopeptidases, for the hydrolysis of the usual ACE synthetic substrate benzoylglycyl-histidyl-leucine (HHL) investigating the possible interference by CPA in the determination of ACE activity in biological fluids. hippuryl-histidyl-leucine 164-194 angiotensin I converting enzyme Homo sapiens 140-143 3030460-5 1987 KM of human liver ACE, measured using hippuryl-L-histidyl-L-leucine and N-benzyloxycarbonyl-L-phenylalanyl-L-histidyl-L-leucine as substrates, was 5 mM and 0.1 mM, respectively. hippuryl-histidyl-leucine 38-67 angiotensin I converting enzyme Homo sapiens 18-21 3038613-1 1987 Angiotensin I-converting enzyme (ACE) activity was measured with hippurylhistidylleucine as a substrate in isolated human glomeruli. hippuryl-histidyl-leucine 65-88 angiotensin I converting enzyme Homo sapiens 0-31 3038613-1 1987 Angiotensin I-converting enzyme (ACE) activity was measured with hippurylhistidylleucine as a substrate in isolated human glomeruli. hippuryl-histidyl-leucine 65-88 angiotensin I converting enzyme Homo sapiens 33-36 2175927-5 1990 Synthetic acylated tripeptides such as radiolabelled hippuryl-histidyl-leucine and hippuryl-glycyl-glycine have been found to be the most suitable substrates for determining the activity of ACE with radiochemical assays. hippuryl-histidyl-leucine 53-78 angiotensin I converting enzyme Homo sapiens 190-193 34097042-5 2021 ACE phenotyping includes (a) determination of ACE activity with 2 substrates (Z-Phe-His-Leu (ZPHL) and Hip-His-Leu (HHL)), (b) calculation of a ratio for hydrolysis of ZPHL and HHL, and (c) quantification of ACE immunoreactive protein levels and ACE conformation with a set of monoclonal antibodies (mAbs) to ACE. hippuryl-histidyl-leucine 103-114 angiotensin I converting enzyme Homo sapiens 0-3 34097042-5 2021 ACE phenotyping includes (a) determination of ACE activity with 2 substrates (Z-Phe-His-Leu (ZPHL) and Hip-His-Leu (HHL)), (b) calculation of a ratio for hydrolysis of ZPHL and HHL, and (c) quantification of ACE immunoreactive protein levels and ACE conformation with a set of monoclonal antibodies (mAbs) to ACE. hippuryl-histidyl-leucine 103-114 angiotensin I converting enzyme Homo sapiens 46-49 6087781-2 1984 ACE activity in serum was measured by its in vitro ability to cleave hippuric acid from the synthetic tripeptide hippuryl-L-histidyl-L-leucine. hippuryl-histidyl-leucine 113-142 angiotensin I converting enzyme Homo sapiens 0-3 3020342-4 1986 Angiotensin-converting enzyme activity was measured by a radiometric assay using [Glycine-1-14C] Hippuryl-L-histidyl-L-leucine (1.1 mmol/L) as substrate, and was expressed as nmol hippuric acid formed per minute/mg protein. hippuryl-histidyl-leucine 97-126 angiotensin I converting enzyme Homo sapiens 0-29 3017438-7 1986 The Km with respect to hippuryl-L-histidyl-L-leucine was 1.9 mM in the case of lung angiotensin-converting enzyme and 1.7 mM in that of kidney angiotensin-converting enzyme, while for the substrate angiotensin I Km values were 62 microM and 76 microM, respectively. hippuryl-histidyl-leucine 23-52 angiotensin I converting enzyme Homo sapiens 84-113 3017438-7 1986 The Km with respect to hippuryl-L-histidyl-L-leucine was 1.9 mM in the case of lung angiotensin-converting enzyme and 1.7 mM in that of kidney angiotensin-converting enzyme, while for the substrate angiotensin I Km values were 62 microM and 76 microM, respectively. hippuryl-histidyl-leucine 23-52 angiotensin I converting enzyme Homo sapiens 143-172 6095490-1 1984 The angiotensin converting enzyme (ACE) activity in the plasma collected from normotensive and hypertensive patients was measured chromatographically by two different methods using hippuryl-histidyl-leucine (HHL-ACE) and synthetic angiotensin I (AI-ACE) as substrates. hippuryl-histidyl-leucine 181-206 angiotensin I converting enzyme Homo sapiens 4-33 6095490-1 1984 The angiotensin converting enzyme (ACE) activity in the plasma collected from normotensive and hypertensive patients was measured chromatographically by two different methods using hippuryl-histidyl-leucine (HHL-ACE) and synthetic angiotensin I (AI-ACE) as substrates. hippuryl-histidyl-leucine 181-206 angiotensin I converting enzyme Homo sapiens 35-38 6298259-2 1982 Samples were incubated with hippurylhistidylleucine, an artificial substrate of angiotensin-converting enzyme. hippuryl-histidyl-leucine 28-51 angiotensin I converting enzyme Homo sapiens 80-109 6304422-1 1983 Angiotensin-converting enzyme (ACE) was assayed spectrophotometrically with hippuryl-histidyl-leucine as substrate. hippuryl-histidyl-leucine 76-101 angiotensin I converting enzyme Homo sapiens 0-29 6304422-1 1983 Angiotensin-converting enzyme (ACE) was assayed spectrophotometrically with hippuryl-histidyl-leucine as substrate. hippuryl-histidyl-leucine 76-101 angiotensin I converting enzyme Homo sapiens 31-34 6304422-8 1983 Lysis of hippuryl-histidyl-leucine by the pancreas and pancreatic juice resulted from an enzyme believed to be carboxypeptidase A which is present as a zymogen and activated by trypsin; this activity differed from ACE in that it had a smaller molecular weight (25,000) compared with ACE of serum (240,000), and it was not strongly inhibited by ethylenediaminetetraacetic acid or SQ 20881 (a specific ACE inhibitor). hippuryl-histidyl-leucine 9-34 angiotensin I converting enzyme Homo sapiens 214-217 6304422-8 1983 Lysis of hippuryl-histidyl-leucine by the pancreas and pancreatic juice resulted from an enzyme believed to be carboxypeptidase A which is present as a zymogen and activated by trypsin; this activity differed from ACE in that it had a smaller molecular weight (25,000) compared with ACE of serum (240,000), and it was not strongly inhibited by ethylenediaminetetraacetic acid or SQ 20881 (a specific ACE inhibitor). hippuryl-histidyl-leucine 9-34 angiotensin I converting enzyme Homo sapiens 283-286 6304422-8 1983 Lysis of hippuryl-histidyl-leucine by the pancreas and pancreatic juice resulted from an enzyme believed to be carboxypeptidase A which is present as a zymogen and activated by trypsin; this activity differed from ACE in that it had a smaller molecular weight (25,000) compared with ACE of serum (240,000), and it was not strongly inhibited by ethylenediaminetetraacetic acid or SQ 20881 (a specific ACE inhibitor). hippuryl-histidyl-leucine 9-34 angiotensin I converting enzyme Homo sapiens 283-286 222502-4 1979 After reaction of 10 microL of untreated serum with the angiotensin-converting enzyme substrate analog hippuryl-L-histidyl-L-leucine, the hippuric acid produced is extracted into ethyl acetate and quantitated, relative to an added internal standard, by liquid chromatography. hippuryl-histidyl-leucine 103-132 angiotensin I converting enzyme Homo sapiens 56-85 6153302-1 1980 The activity of angiotensin-converting enzyme in human prostate was measured by spectrophotometric method using Hippuryl-L-histidyl-L-leucine (Hip-His-Leu) as substrate. hippuryl-histidyl-leucine 112-141 angiotensin I converting enzyme Homo sapiens 16-45 227623-1 1979 The method of chemical assay of angiotensin I-converting enzyme described is a modification of the previously published spectrophotometric assay based on quantitation of hippuric acid released from hippuryl-L-histidyl-L-leucine. hippuryl-histidyl-leucine 198-227 angiotensin I converting enzyme Homo sapiens 32-63 211845-1 1978 Using hippuryl-L-histidyl-L-leucine as substrate, serum angiotensin-converting enzyme was measured in 13 patients who had adult respiratory distress syndrome, eight patients with respiratory failure without adult respiratory distress syndrome, and two groups of controls: 24 healthy blood donors and 24 hospitalized patients with a variety of conditions but without respiratory failure or adult respiratory distress syndrome. hippuryl-histidyl-leucine 6-35 angiotensin I converting enzyme Homo sapiens 56-85 233224-1 1979 Serum angiotensin converting enzyme activity was measured in 60 blood donors and 100 patients with sarcoidosis histologically confirmed using a spectrophotometric assay with hippurylhistidylleucine as substrate. hippuryl-histidyl-leucine 174-197 angiotensin I converting enzyme Homo sapiens 6-35 30391811-4 2019 The enzymatic activity of the ACE-MB was validated based on its Michaelian kinetic behavior towards hippuryl-histidyl-leucine by UHPLC-MS/MS method firstly. hippuryl-histidyl-leucine 100-125 angiotensin I converting enzyme Homo sapiens 30-33 191959-1 1977 Using hippuryl-L-histidyl-L-leucine as a substrate analog, serum angiotensin converting enzyme (ACE) was spectrophotometrically estimated in patients with bronchial asthma. hippuryl-histidyl-leucine 6-35 angiotensin I converting enzyme Homo sapiens 65-94 74963-1 1978 Using hippuryl-L-histidyl-L-leucine as a substrate analogue, serum angiotensin converting enzyme (ACE) was spectrophotometrically estimated in patients with bronchial asthma. hippuryl-histidyl-leucine 6-35 angiotensin I converting enzyme Homo sapiens 67-96 74963-1 1978 Using hippuryl-L-histidyl-L-leucine as a substrate analogue, serum angiotensin converting enzyme (ACE) was spectrophotometrically estimated in patients with bronchial asthma. hippuryl-histidyl-leucine 6-35 angiotensin I converting enzyme Homo sapiens 98-101 201593-1 1977 The activity of serum angiotensin converting enzyme (ACE), assayed fluorometrically with the substrate hippuryl-L-histidyl-L-leucine was significantly higher in 116 patients with sarcoidosis than in 415 patients with other diseases--pulmonary and nonpulmonary--and in 58 normal subjects. hippuryl-histidyl-leucine 103-132 angiotensin I converting enzyme Homo sapiens 22-51 201593-1 1977 The activity of serum angiotensin converting enzyme (ACE), assayed fluorometrically with the substrate hippuryl-L-histidyl-L-leucine was significantly higher in 116 patients with sarcoidosis than in 415 patients with other diseases--pulmonary and nonpulmonary--and in 58 normal subjects. hippuryl-histidyl-leucine 103-132 angiotensin I converting enzyme Homo sapiens 53-56 31131896-8 2019 The intracellular and extracellular ACE activity was measured using hippuryl-His-Leu as substrate via a fluorimetric assay and expression was analyzed using western blot analysis. hippuryl-histidyl-leucine 68-84 angiotensin I converting enzyme Homo sapiens 36-39 29641461-2 2018 The IC50 value of the peptide was 233.178 muM, which was determined by the high performance liquid chromatography method by measuring the amount of hippuric acid (HA) generated from the ACE decomposition substrate (hippuryl-l-histidyl-l-leucine (HHL) to assess the ACE activity. hippuryl-histidyl-leucine 215-244 angiotensin I converting enzyme Homo sapiens 186-189 23672666-3 2013 Extending our recent molecular dynamics simulation of the testis ACE in complex with a bona fide substrate molecule, hippuryl-histidyl-leucine, we presented here a detailed investigation of the hydrolytic process and possible influences of the chloride ion on the reaction using a combined quantum mechanical and molecule mechanical method. hippuryl-histidyl-leucine 117-142 angiotensin I converting enzyme Homo sapiens 65-68 27184002-6 2016 The hydrolysis of hippuryl-histidyl-leucine (HHL) as catalyzed by the N-domain of human somatic ACE was explored, and the effects of chloride ion on the overall reaction were also investigated. hippuryl-histidyl-leucine 18-43 angiotensin I converting enzyme Homo sapiens 96-99