Biomedical subjects

G M Pacifici

Publications and source records attributed to G M Pacifici.

At least 55 records · Page 3Linked to original sources

PubMed1993

Interindividual variability of phenol- and catechol-sulphotransferases in platelets from adults and newborns.

1 Phenol- and catechol- sulphotransferase activities were measured with p-nitrophenol and dopamine as substrates in platelets obtained from 100 newborns and 100 healthy adults. 2 Mean +/- (s.d.) estimates of catechol sulphotransferase activity were 7.07 +/- 5.93 (adult) and 13.3 +/- 6.42 (newborn) pmol min(-1) mg(-1) protein, respectively (P < 0.001). The coefficients of variation were 84% (adult) and 48% (newborn). The frequency distribution of sulphotransferase activity was symmetric and did not deviate significantly from normality in newborn platelets, but was positively skewed in adult platelets. 3 Mean +/- (s.d.) estimates of phenol sulphotransferase activity were 3.01 +/- 3.21 (adult) and 4.80 +/- 4.34 (newborn) pmol min(-1) mg(-1), respectively (P < 0.001). The coefficients of variation were 107% (adult) and 90% (newborn). The frequency distribution of sulphotransferase activity was positively skewed in both newborn and adult platelets. 4 Since sulphotransferase activity in platelets is well-expressed at birth and a prenatal development of sulphotransferase has been described in mid-gestational human foetal liver, the newborn should be able to sulphate drugs.

Adult↗

PubMed1993

S-methyltransferases in human intestine: differential distribution of the microsomal thiol methyltransferase and cytosolic thiopurine methyltransferase along the human bowel.

1. The activities of the microsomal thiol methyltransferase and the cytosolic thiopurine methyltransferase were measured with 2-mercaptoethanol and 6-mercaptopurine as substrates in human ileum, ascending colon, transverse colon, descending colon and liver. 2. Thiol methyltransferase activity (pmol/min per mg) (mean +/- SD) was 495 +/- 280 (ileum), 786 +/- 454 (ascending colon), 1791 +/- 233 (transverse colon), 964 +/- 484 (descending colon) and 4800 +/- 1194 (liver). 3. Thiopurine methyltransferase (pmol/min per mg) (mean +/- SD) was 53.5 +/- 15.4 (ileum), 34.6 +/- 11.4 (ascending colon), 64.3 +/- 12.1 (transverse colon), 57.0 +/- 10.1 (descending colon) and 106 +/- 20.4 (liver). 4. Transferase in intestinal mucosa followed non-Michaelis-Menten kinetics, and two phases representing high and low affinity forms, for the acceptor methyl substrates were observed. 5. Comparison of intestinal with hepatic activities showed that thiopurine methyltransferase is better expressed than thiol methyltransferase in the human intestine, at least with the substrates studied.

Adult↗

PubMed1993

Conjugation of benzoic acid with glycine in human liver and kidney: a study on the interindividual variability.

1. The rate of conjugation of benzoic acid with glycine was measured in the homogenates of 110 specimens of human liver and in 67 specimens of human renal cortex. 2. The assay for the formation of benzoyl glycine consisted of measuring the formation of benzoyl glycine from (14C) benzoic acid and glycine in the presence of coenzyme A and ATP. 3. In human liver, the mean (+/- SD) and coefficient of variation for the formation rate of benzoyl glycine were 254 +/- 90.5 nmol min-1 per g liver and 36%, respectively. There was a weak, but significant, negative correlation (r = -0.339, p < 0.001) between the rate of formation of benzoyl glycine and the liver donor's age. 4. In the human kidney, the rate of benzoyl glycine formation was normally distributed. The mean (+/- SD) and coefficient of variation were 321 +/- 99.3 nmol min-1 per g kidney and 31%, respectively. 5. These in vitro results are consistent with the view that the in vivo rate of conjugation of carboxylic acid with glycine varies among subjects and is normally distributed.

Adult↗

PubMed1992

Interindividual variability in the N-sulphation of desipramine in human liver and platelets.

1. The activity of N-sulphotransferase (N-ST) with desipramine (DMI) as substrate was measured in 118 human liver specimens, in platelets obtained from 105 subjects, in 12 specimens of human ileum and colon mucosa and in five specimens of human kidney and lung. 2. N-ST activity ranged between 5.71 and 157 pmol min-1 mg-1 protein in human liver and between 0.27 and 17.3 pmol min-1 mg-1 protein in human platelets. 3. Probit analysis was compatible with a unimodal distribution of the data from both liver and platelets. 4. The frequency distribution histograms of N-ST were asymmetric, with a positive skew in data from both liver and platelets. The mode, median and mean of N-ST were 16.4, 30.2 and 40.4 pmol min-1 mg-1 protein in liver, and 2.12, 3.61 and 3.82 pmol min-1 mg-1 protein in platelets, respectively. After logarithmic transformation of N-ST activity, the frequency distribution histogram was symmetric for data from both liver and platelets. 5. In extrahepatic tissues, the average (+/- s.d.) N-ST activity (pmol min-1 mg-1 protein) was 22.2 +/- 22.8 (ileum), 20.9 +/- 26.9 (colon), 12.4 +/- 5.5 (renal cortex), 9.3 +/- 2.8 (renal medulla) and 4.2 +/- 1.1 (lung). N-ST is widely distributed in the body and the intestine is the extrahepatic tissue with the highest N-ST activity.

Adult↗

PubMed1992

The effect of ageing on plasma albumin and plasma protein binding of diazepam, salicylic acid and digitoxin in healthy subjects and patients with renal impairment.

1. Plasma albumin concentration was measured in 118 healthy subjects (aged between 18 and 87 years), in 95 renal patients with creatinine clearances between 15 and 50 ml min-1 (aged between 14 and 79 years) and in 101 uraemic patients maintained on chronic haemodialysis (aged between 27 and 83 years). 2. There was a significant (P less than 0.001) negative correlation between albumin concentration and age in healthy subjects, but no correlation in patients with low creatinine clearance or in uraemic patients. 3. The ex vivo plasma binding of diazepam (1 microM), salicylic acid (2 mM) and digitoxin (37 nM) was studied in groups of age-selected young and aged healthy subjects in patients with low creatinine clearance and in patients with uraemia. The unbound fractions of diazepam and salicylic acid were about double in old compared with young healthy subjects whereas they were similar in young and old patients with lowered creatinine clearance. In uraemic patients, ageing did not affect the binding of salicylic acid whereas the unbound fraction of diazepam was slightly but significantly greater in elderly subjects. The unbound fraction of digitoxin was independent of age in both healthy subjects and in those with renal disease. 4. Decreased plasma binding of diazepam and salicylic acid was partially corrected by extensive dialysis of plasma. The lower plasma binding of diazepam and salicylic acid associated with ageing may be ascribed to the effects of endogenous displacers and to hypoalbuminaemia. The influence of these two factors appears to be drug-dependent.

Adolescent↗

PubMed1992

Histamine N-methyl transferase: inhibition by drugs.

1. Histamine N-methyl transferase activity was measured in samples of human liver, brain, kidney, lung and intestinal mucosa. The mean (+/- s.d.) rate (nmol min-1 mg-1 protein) of histamine N-methylation was 1.78 +/- 0.59 (liver, n = 60), 1.15 +/- 0.38 (renal cortex, n = 8), 0.79 +/- 0.14 (renal medulla, n = 8), 0.35 +/- 0.08 (lung, n = 20), 0.47 +/- 0.18 (human intestine, n = 30) and 0.29 +/- 0.14 (brain, n = 13). 2. Inhibition of histamine N-methyl transferase by 15 drugs was investigated in human liver. The IC50 for the various drugs ranged over three orders of magnitude; chloroquine was the most potent inhibitor. 3. The average IC50 values for chloroquine were 12.6, 22.0, 19.0, 21.6 microM in liver, renal cortex, brain and colon, respectively. These values are lower than the Michaelis-Menten constant for histamine N-methyltransferase in liver (43.8 microM) and kidney (45.5 microM). Chloroquine carried a mixed non-competitive inhibition of hepatic histamine N-methyl transferase. Some side-effects of chloroquine may be explained by inhibition of histamine N-methyl transferase.

Adult↗

PubMed1992

Cigarette smoke inhibits cytosolic but not microsomal epoxide hydrolase of human lung.

The effect of cigarette smoke exposure on the activity of cytosolic and microsomal epoxide hydrolase (EH) has been investigated in human lung. Patients were classified as 'recent smokers' (n = 9) or 'non-recent smokers' (n = 10) according to whether they were or were not still smoking 1 month before surgery. Cytosolic EH was measured with [3H]trans-stilbene oxide as a substrate, whereas microsomal EH was measured with [7-3H]styrene oxide as a substrate. Microsomal EH activity did not differ between recent smokers (2.51 +/- 0.93 nmol min-1 mg-1) and non-recent smokers (2.74 +/- 1.10 nmol min-1 mg-1), whereas cytosolic EH activity was significantly lower in recent smokers (6.46 +/- 1.79 pmol min-1 mg-1) than in non-recent smokers (8.41 +/- 2.09 pmol min-1 mg-1, P less than 0.05). Cytosolic EH activity was correlated with the number of days that had passed since the cessation of smoking (r = 0.58, P less than 0.05) and the effect was dose-dependent, since the enzyme activity was inversely correlated with the number of cigarettes smoked per day (r = 0.85, P less than 0.01). This suggests that recent smoking exposure inhibits the activity of cytosolic EH but not microsomal EH, and that the inhibition increases with the number of cigarettes smoked per day. The contribution of cytosolic enzymes to xenobiotic metabolism may be remarkable in extrahepatic tissues. The inhibition of cytosolic EH by tobacco smoke may reduce the inactivation of carcinogenic epoxides in human lung tissues and so may increase a person's susceptibility to lung cancer.

Adult↗

PubMed1992

Methods of determining plasma and tissue binding of drugs. Pharmacokinetic consequences.

The available techniques for the investigation of drug binding to plasma and tissues protein are reviewed and the advantages and disadvantages of the various techniques stated. A comparison of different plasma protein binding techniques is made which shows that the size of the unbound fraction of drug may be influenced by the method used. Protein binding may be assayed by methods including equilibrium dialysis, ultrafiltration, ultracentrifugation, gel filtration, binding to albumin microspheres and circular dichroism. Tissue binding techniques can involve testing binding to isolated organs, tissue slices, homogenates and isolated subcellular particles. Details of the available methods to compute pharmacokinetic constants are given. Stereoselective binding has been investigated for a limited number of drugs and the difference in the binding of 2 enantiomers is usually modest. The measurement of the binding constants is often required to characterise the drug-protein interaction. Mathematical and graphical methods to compute the pharmacokinetic parameters are discussed. The implications of binding on the volume of distribution and clearance of drugs are examined.

Animals↗

PubMed1992

Quantitative contribution of endogenous compounds and hypoalbuminemia in reducing the binding of furosemide in the plasma of newborn infants.

The protein binding of furosemide was studied in the plasma of newborn infants and adult subjects. Plasma consisted of two pools obtained from 25 newborns and adult subjects. The concentrations of albumin were 36.8 (newborn) and 48.3 g/l (adult). The unbound fraction of furosemide was 1.38 +/- 0.15 (adult) and 2.03 +/- 0.13% (newborn; p < 0.001). After extensive dialysis of the plasma, the unbound fraction of furosemide was 1.12 +/- 0.15 (adult) and 1.39 +/- 0.09% (newborn; p < 0.0001), suggesting that dialyzable endogenous compounds interfere with the binding of furosemide. The addition of human albumin to the newborn plasma to give a final albumin concentration of 48.3 g/l yielded an unbound fraction of furosemide of 1.63 +/- 0.08 (nondialyzed plasma) and 1.17 +/- 0.08% (dialyzed plasma; p < 0.0001). The addition of albumin to the dialyzed newborn plasma, to give a final albumin concentration similar to that in adult plasma, decreased the unbound furosemide to the level of the dialyzed adult plasma. The binding defect of furosemide in newborn plasma reflects either the effects of the endogenous inhibitors or of hypoalbuminemia. The intrinsic binding properties for furosemide of newborn dialyzed plasma are similar to those of dialyzed adult plasma. This consideration corroborates our previous results on the binding of furosemide and diazepam, salicylic acid and digitoxin to newborn and adult albumin. The displacement of furosemide by salicylic acid, tolbutamide and azapropazone is 70% greater in newborn than in adult plasma. The greater displacing effect is largely due to hypoalbuminemia.

Aging↗

PubMed1992

Interindividual variability in the concentrations of albumin and alpha-1-acid glycoprotein in patients with renal or liver disease, newborns and healthy subjects: implications for binding of drugs.

The concentrations of human plasma albumin (HPA) and alpha-1-acid glycoprotein (AAG) were measured in the serum obtained from 84 healthy subjects, 56 umbilical cords, 41 patients with renal failure, 65 patients maintained on chronic hemodialysis and 46 patients with liver cirrhosis. Severity of liver dysfunction was assessed with the use of Pugh et al. [1973] classification. Of the cirrhotic patients, 12, 22 and 12 patients were classified as mild, moderate and severe liver dysfunction, respectively. The coefficient of variation of AAG was greater than HPA in all groups of subjects, and the variability of HPA and AAG is increased in patients compared to healthy subjects. As the liver dysfunction progresses, HPA concentration decreases whereas, the average AAG concentration is not changed in mild, moderate and severe liver dysfunction. The coefficients of variation for HPA and AAG in moderate and severe liver disease is over twice those for healthy subjects. The concentration of HPA is normally distributed in all groups of subjects, with the exception of the cord serum. The frequency distribution of AAG was normal in healthy subjects whereas, it was asymmetric, being positively skewed, in newborn, in renal and liver patients. The wide interindividual variability and the not-normal frequency distribution of AAG in liver or renal patients make its mean of little value in defining a group. Neither HPA nor AAG correlated with the clearance of creatinine in renal patients. In liver disease, HPA and AAG did not correlate with GPT and GOT activities, prothrombinic activity and bilirubin concentration. HPA did not correlate with AAG in any group.

Adolescent↗

PubMed1991

Distribution of UDP-glucuronosyltransferase and its endogenous substrate uridine 5'-diphosphoglucuronic acid in human tissues.

The activity of UDP-glucuronosyltransferase (UDPGT) and the concentration of its endogenous substrate, 5'-diphosphoglucuronic acid (UDPGA), have been measured in human liver, kidney, lung and intestinal mucosa. The activity of UDPGT was tissue- and substrate-dependent. The liver/kidney and liver/intestine ratios for UDPGT varied over one order of magnitude with three substrates. The highest activity of UDGPT in extrahepatic tissues was in the kidney, with 1-naphthol as substrate; it was about half of the hepatic activity. The concentration (mumol.kg-1) of UDPGA was 279 (liver), 17.4 (kidney), 19.3 (intestinal mucosa) and 17.2 (lung), it was at least 15-fold higher in liver than the other tissues, and the concentration in kidney, lung and intestinal mucosa was similar. The kinetics of UDPGT in a liver homogenate at varying concentrations of UDPGA and fixed concentration of 1-naphthol, ethinyloestradiol, and morphine was also measured. The apparent kM for UDPGT depended upon the chemical nature of the UDPGA-acceptor substrate; average values of kM were 63, 300, and 700 mumol.l-1 for 1-naphthol, ethinyloestradiol and morphine respectively. These values are, respectively, lower, similar to and higher than the hepatic concentration of UDPGA. Under certain circumstances UDPGA may be the limiting factor in the in vivo glucuronidation of drugs by extrahepatic tissues.

Adult↗

PubMed1991

Chloroform bioactivation by microsomes from colonic and ileal mucosa of rat and man.

The cytochrome P-450 system present in colonic and small-intestinal mucosal microsomes from control and beta-naphthoflavone pretreated rats is not able to catalyze the biotransformation of chloroform either oxidatively or reductively. Anoxic incubations of 14CHCl3 with mucosal microsomes obtained from human colon and ileum biopsies resulted in significant levels of covalent binding to lipids but not to protein; no covalent binding was measured after room-air-equilibrated incubations. The bioactivation of CHCl3 by human colonic mucosal microsomes can therefore occur in conditions which may be representative of the physiologically low oxygenation of the outer layers of this tissue. These results support the possibility of an association between colonic cancer and exposure to CHCl3, claimed in some epidemiological studies, but not evident from studies of laboratory animals.

Animals↗

PubMed1991

Interindividual variability in the glucuronidation and sulphation of ethinyloestradiol in human liver.

1. Glucuronidation and sulphation of ethinyloestradiol (EE2) was studied in human liver. Microsomal glucuronyltransferase activity was measured in 110 livers whose donors were 71 women and 39 men. Enzyme activity ranged between 12.6 and 242 pmol min-1 mg-1 protein, i.e. over a 19-fold range and the mean (+/- s.d.) glucuronyltransferase activity was 96.8 +/- 47.9 pmol min-1 mg-1 protein. 2. Cytosolic sulphotransferase activity was measured in 138 livers whose donors were 90 women and 48 men. Enzyme activity ranged between 14.4 and 98.2 pmol min-1 mg-1 protein, i.e. over a 7-fold range, and the mean (+/- s.d.) sulphotransferase activity was 43.7 +/- 18.6 pmol min-1 mg-1 protein. 3. Human liver glucuronyltransferase and sulphotransferase activities showed a unimodal distribution pattern. Enzyme activities were neither sex-related nor age-dependent. Sulphotransferase activity did not correlate with glucuronyltransferase activity (n = 80) suggesting that the two enzymes are independently regulated. The ratio of specific glucuronyltransferase to sulphotransferase activity ranged between 0.15 and 8.0 (mean +/- s.d., 2.44 +/- 1.51) and was unimodally distributed.

Adult↗

PubMed1991

Thiol methyltransferase in humans: development and tissue distribution.

Thiol methyltransferase (EC 2.1.1.9, TMT) activity was measured with 2-mercaptoethanol in the microsomal fraction of 12 placenta and 31 fetal and 33 adult liver specimens. TMT activity (nmol/min incubation/mg protein; mean +/- SD) was 0.61 +/- 0.25 (placenta), 0.74 +/- 0.45 (fetal liver), and 4.51 +/- 2.29 (adult liver). TMT activity was also measured in extrahepatic tissues and it was about one order of magnitude lower in fetal lungs, kidney and intestine as compared with the fetal liver. A similar distribution pattern was also observed in adult tissues except that in the kidney TMT activity was one third of the hepatic one. Studies of enzyme kinetics showed that fetal and adult hepatic TMT obeyed non-Michaelis-Menten kinetics when 2-mercaptoethanol was the varying substrate. Average values of Km for the higher and lower affinity phases were 0.03 and 14.05 mmol/l, respectively (fetal liver) and 0.005 and 14.57 mmol/l, respectively (adult liver). This paper shows that TMT develops prenatally and its distribution pattern is consistent with that of other microsomal enzymes, being preferentially associated with the liver both in the human fetus and in adult subject.

Adult↗

PubMed1991

Thiopurine methyltransferase in humans: development and tissue distribution.

Thiopurine methyltransferase (EC 2.1.1.67, TPMT) was studied with 6-mercaptopurine as substrate in the cytosolic fraction from 18 human fetal liver, 16 placental and 22 adult liver specimens. TPMT activity (pmol x min-1 x mg-1; mean +/- SD) was 33.2 +/- 15.8 (fetal liver), 19.5 +/- 11.1 (placenta) and 105 +/- 57.1 (adult liver). Fetal liver activity of TPMT is one third that in adult liver suggesting that this enzyme is well developed in the mid-gestational human fetus. The distribution of TPMT seems to be ubiquitous both in the fetus and adult subject. The kidney is an important site of methylation as suggested by the renal activity of TPMT (197 +/- 70 pmol x min-1 x mg-1) which is twice as high as the hepatic one. Fetal and adult hepatic TPMT obey nonmichaelian kinetics. Two phases, one with lower and one with higher affinity for 6-mercaptopurine, were observed. The average Km for the high affinity phase was 0.12 mmol/l (fetus) and 0.13 mmol/l (adult), whereas the Km for the lower affinity phase was 1.79 mmol/l (fetus) and 1.42 mmol/l (adult). This paper shows that TPMT develops before the second trimester of gestation in human fetus, that it has an ubiquitous distribution in the human fetus and adult subjects and the kinetic pattern of this enzyme is consistent in fetal and adult liver.

Adolescent↗

PubMed1991

Conjugation of benzoic acid with glycine in the human fetal and adult liver and kidney.

The rate of hippuric acid formation was measured in the homogenates obtained from 26 specimens of human adult liver, 9 specimens of human mid-gestational fetal liver, 5 specimens of human adult kidney and 11 specimens of human mid-gestational fetal kidney. The average (pmol/min/mg tissue +/- SD) rate of hippuric acid formation was 322 +/- 99 (adult liver), 7.6 +/- 3.6 (fetal liver), 284 +/- 117 (adult kidney) and 6.4 +/- 6.7 (fetal kidney). One third of the fetal livers and kidneys studied were inactive in the formation of hippuric acid. These findings indicate that the conjugation of carboxylic acid with glycine is poorly developed in the mid-gestational human fetus. The kinetics of the formation of hippuric acid were studied in 3 fetal and adult livers and also in 3 fetal kidneys and in 3 specimens of the cortex and medulla of adult kidneys. The transformation of the data into Eadie-Hofstee plots generated straight lines in fetal and adult livers and kidneys. The Michaelis-Menten constant for the formation of hippuric acid (mean +/- SD, mM) was 43.4 +/- 6.6 (adult liver), 27.3 +/- 10.1 (fetal liver), 33.3 +/- 6.1 (adult renal cortex), 34.7 +/- 11.3 (adult renal medulla) and 15.3 +/- 3.5 (fetal kidney). The maximum velocity of the reaction (mean +/- SD, pmol/min/mg tissue) was 204 +/- 47.8 (adult liver), 6.0 +/- 1.3 (fetal liver), 199 +/- 40.7 (adult renal cortex), 24.2 +/- 16.9 (adult renal medulla) and 6.4 +/- 1.8 (fetal kidney). The inhibitory effect of 8 drugs containing a carboxylic acid group on the rate of hippuric acid formation was studied in 3 adult livers. Salicylic acid and diflunisal were the most powerful as inhibitors. Ibuprofen, furosemide and sodium valproate were weak inhibitors, whereas ketoprofen, naproxen and captopril did not inhibit the formation of hippuric acid. The IC50 values (mean +/- SD) of salicylic acid and diflunisal on the rate of hippuric acid formation were 0.19 +/- 0.05 and 1.18 +/- 0.19 mM, respectively.

Acyltransferases↗

PubMed1991

Binding of diazepam, salicylic acid and digitoxin to albumin isolated from fetal and adult serum.

Albumin was isolated from pooled fetal serum obtained at normal delivery at term and from pooled adult plasma. Albumin isolation was carried out by means of PEG precipitation followed by ion exchange chromatography on DEAE-Sephadex A 50 and then on SP-Sephadex C 50. The binding of diazepam (1 microM), salicylic acid (2 mM) and digitoxin (6 nM) to albumin (40 g/l) was measured by equilibrium dialysis at 37 degrees C. The unbound fraction (mean +/- SD) for fetal and adult albumin of diazepam was 1.86 +/- 0.24 and 1.82 +/- 0.15% (NS), that of digitoxin was 3.18 +/- 0.27 and 3.36 +/- 0.04% (NS) and that of salicylic acid was 11.65 +/- 0.99 and 9.47 +/- 0.75% (p less than 0.05), respectively. With both fetal and adult albumin, a single class of binding sites was observed for diazepam and digitoxin, whereas two classes of binding sites were observed for salicylic acid. The number of binding sites (n, moles of drug per mole of albumin) for fetal and adult albumin was 0.83 and 1.02 for diazepam and 0.014 and 0.018 for digitoxin, respectively. For salicylic acid, n was 1.45 (fetal albumin) and 1.55 (adult albumin) for the higher affinity site, and 3.06 (fetal albumin) and 3.27 (adult albumin) for the lower affinity site. The association constant (Ka, M-1) for diazepam was 1.36 x 10(5) (fetal albumin) and 1.00 x 10(5) (adult albumin) and that for digitoxin was 4.12 x 10(6) (fetal albumin) and 2.7 x 10(6) (adult albumin). For salicylic acid, Ka was 38.4 x 10(3) (fetal albumin) and 35.8 x 10(3) (adult albumin) for the higher affinity site, and 2.7 x 10(3) (fetal albumin) and 4.3 x 10(3) (adult albumin) for the lower affinity site. This work shows that fetal and adult albumin have similar binding properties and corroborates our previous findings with furosemide.

Adult↗

PubMed1991

Human liver sulphotransferase and UDP-glucuronosyltransferase: structure-activity relationship for phenolic substrates.

1. Human liver sulphotransferase and UDP-glucuronosyltransferase were studied with phenol, methyl-, ethyl-, propyl-, butyl-, phenyl-, nitro-, amino-phenols and hydroxybenzoic acids as substrates. 2. The Michaelis-Menten constants (Km) and the maximum velocities of reaction (Vmax) of sulphotransferase and UDP-glucuronosyltransferase for each substrate were measured. 3. The Km values for sulphotransferase varied over 5000-fold whereas they varied over 25-fold for UDP-glucuronosyltransferase. 4. Sulphotransferase and UDP-glucuronosyltransferase have different structure-activity relationships with phenolic substrates.

Adult↗