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PubMed2001

Leukemia inhibitory factor decreases the arylamine N-acetyltransferase activity in human cumulus granulosa cells.

PURPOSE: To evaluate the activities of acetyl coenzyme A (AcCoA):arylamine N-acetyltransferase (NAT) of intact cumulus granulosa cells and the role of leukemia inhibitory factor (LIF) upon their NAT activities. METHODS: Thirty women accepted controlled ovarian hyperstimulation (COH) and oocyte retrievals. Human cumulus granulosa cells were obtained during oocyte retrievals. Using 2-aminofluorene (2-AF) and p-aminobenzoic acid (PABA) as substrates, NAT activity of all samples was determined by high pressure liquid chromatography. After the incubation with different time and concentrations of 2-AF, PABA, and LIF, 2-acetyl-aminofluorene (2-AAF) and N-acetyl-PABA (N-Ac-PABA) were measured. RESULTS: After incubation with 2.812, 5.625, 11.25, and 22.5 microM of 2-AF/PABA, their product concentrations (2-AAF/N-Ac-PABA) were 0.42/0.32, 0.76/0.58, 1.29/1.04, and 1.94/1.26 nmol/10(6) cells, respectively. After 6, 12, 18, and 24 h incubation with 11.25 microM of 2-AF/PABA, their product concentrations were 0.19/0.12, 0.56/0.4, 0.98/0.79, and 1.3/1.0 nmol/10(6) cells, respectively. After incubation with 0, 5, and 50 microM of LIF, the 2-AAF/N-Ac-PABA concentrations were 0.98/0.80, 0.70/0.52, and 0.49/0.30 nmol/10(6) cells, respectively. CONCLUSION: Intact human cumulus granulosa cells could acetylate arylamine carcinogen (2-AF) and noncarcinogens drug (PABA). LIF decreased the NAT activities. It provides a model for monitoring the effects of COH and LIF upon the oocytes.

2-Acetylaminofluorene↗
PubMed2001

Kinetics of acetyl coenzyme A: arylamine N-acetyltransferase from rapid and slow acetylator human benign prostatic hyperplasia tissues.

N-acetyltransferase (NAT) activity was determined in 40 human benign prostatic hyperplasia tissues using 2-aminofluorene (AF) and p-aminobenzoic acid (PABA) as substrates. These were then assayed by high performance liquid chromatography for determining the amounts of acetylated AF and PABA and non-acetylated AF and PABA. The activities (mean +/- SD) of AF-NAT from human benign prostatic hyperplasia tissues were divided into rapid (2.06 +/- 0.08 nmol/min per milligram protein), intermediate (1.25 +/- 0.26 nmol/min per milligram protein), and slow (0.58 +/- 0.30 nmol/min per milligram protein) acetylator groups. The activities (mean +/- SD) of PABA-NAT from human benign prostatic hyperplasia tissues were also divided into rapid (2.00 +/- 0.00 nmol/min per milligram protein), intermediate (1.25 +/- 0.18 nmol/min per milligram protein), and slow (0.48 +/- 0.29 nmol/min per milligram protein) acetylator groups. Kinetic constants for arylamine NAT activities were determined for each of these acetylator groups. Apparent differences in Km and Vmax for AF were found. Therefore, there seems to be a polymorphism in NAT activity with two rapid, five intermediate, and 33 slow acetylators among the 40 samples assayed. This is the first demonstration of acetyl CoA-arylamine NAT activity in human benign prostatic hyperplasia tissues.

4-Aminobenzoic Acid↗
PubMed1992

Protective effect of two sunscreens against lethal and genotoxic effects of UVB in V79 Chinese hamster cells and Saccharomyces cerevisiae strains XV185-14C and D5.

Effects of p-aminobenzoic acid (PABA) and of 4-[(2-oxo-3-bornylidene)methyl]-phenyl trimethylammonium methylsulfate (OMM), two components used in sunscreen formulations, on the mutagenicity of UVB irradiation are compared in three genetic assay systems. A haploid strain of Saccharomyces cerevisiae XV185-14C was used to measure reverse mutations at three loci. The diploid strain D5 of Saccharomyces cerevisiae was used to screen for reciprocal mitotic recombination. The induction of forward mutations was measured in Chinese hamster V79 cells. Our results indicate that UVB irradiation induced HGPRT- mutants in V79 cells, reverse mutations in Saccharomyces cerevisiae strain XV185-14C, and mitotic crossing over and other genetic alterations in Saccharomyces cerevisiae strain D5. V79 Chinese hamster lung cells were the most sensitive to UVB irradiation, followed by Saccharomyces cerevisiae haploid strain XV185-14C and the diploid strain D5. PABA and OMM were both capable of protecting all three types of cells from UVB irradiation regarding both lethality and induction of various types of genetic alterations. At higher concentrations (above 10(-5) M), OMM was more effective in its photoprotective effect toward UVB irradiation than PABA.

4-Aminobenzoic Acid↗
PubMed1998

Validation with biological markers for food intake of a dietary assessment method used by Swedish women with three different dietary preferences.

OBJECTIVES: To validate a dietary assessment method, a 4-day food record together with a duplicate portion technique, with biological markers for food intake. DESIGN: Four days of duplicate portions were collected in parallel with food recording. A 24-h urine sample and the faeces corresponding to the food intake (using a coloured marker) were collected. Completeness of urine and faeces collections was assessed using para-aminobenzoic acid (PABA) in urine and cadmium in faeces, respectively. Biomarkers of food intake (energy, protein, fibre, sodium, potassium, calcium) were measured in urine and faeces. SETTING: Swedish west coast. SUBJECTS: Non-smoking Swedish women, 20-50 years of age, consuming a mixed diet (n = 34), a mixed diet rich in shellfish (n = 17) or a vegetarian/high-fibre diet (n = 23). RESULTS: The average ratio (food intake according to the dietary assessment methods/ biological marker) for protein, sodium, potassium and calcium was 0.86. This indicates an underestimation of the food intake by approximately 15%. The ratio of stated fibre intake to biological marker was 1.20 for the mixed diet and the vegetarian diet group, indicating an overestimation by approximately 20%. CONCLUSIONS: The underestimation of the intake of protein, sodium, potassium and calcium by all three groups and the overestimation of the fibre intake by two groups indicate that underreporting is selective to certain nutrients and foods and to various groups of people. The two dependent dietary assessment methods were equally good in measuring protein intake, which indicates that the women recorded what they actually duplicated.

4-Aminobenzoic Acid↗
PubMed2004

Evidence for arylamine N-acetyltransferase activity in Klebsiella pneumoniae.

Arylamine N-acetyltransferase (NAT) enzymes have been found in laboratory animals, humans, microorganisms (fungi, bacteria and parasites), and in plants. But the characteristics of NAT from Klebsiella pneumoniae are not clear. NAT activities with p-aminobenzoic acid (PABA) and 2-aminofluorene (AF) as substrates were examined in the cytosol of K. pneumoniae. NAT activity (N-acetylation of substrates) was determined using an acetyl coenzyme A recycling assay and high performance liquid chromatography for determining the amounts of acetylated or non-acetylated PABA or AF. NAT activities from a number of K. pneumoniae isolates were found to be 0.72 +/- 0.08 nmol/min/mg protein for AF, and 0.49 +/- 0.04 nmol/min/mg protein for PABA. The kinetic parameters of apparent Michaelis constant (Km) and maximum velocity (Vmax) obtained were 2.92 +/- 0.48 mM and 7.89 +/- 0.82 nmol/min/mg protein, respectively, for AF and 2.42 +/- 0.28 mM and 9.87 +/- 0.64 nmol/min/mg protein, respectively, for PABA. The optimal pH value for the NAT activity was 7.0 for AF and PABA. The optimal temperature for NAT activity was 37 degrees C for both substrates. The NAT activity was inhibited by 50% with 0.25 mM iodoacetamide, and by more than 90% at 1.0 mM. Among a series of divalent cations and salts, Cu2+ and Zn2+ were the most potent inhibitors of NAT activity.

4-Aminobenzoic Acid↗
PubMed1999

Correlation between genotype and phenotype of the human arylamine N-acetyltransferase type 1 (NAT1).

Arylamine N-acetyltransferase 1 (NAT1) conjugates several aromatic amines and their N-hydroxylated metabolites by N- or O-acetylation. NAT1 genotype and phenotype is known to be variable in human populations. In this study, we set out to measure the functional relevance of the frequent NAT1 gene variants for the activity in human red blood cells. Healthy German volunteers (N = 314) were genotyped for NAT1 alleles *3, *4, *10, *11, *14, and *15 using polymerase chain reactions and restriction fragment length pattern analysis, and NAT1 enzyme kinetic parameters were measured in a subset of 105 individuals using p-aminobenzoic acid as specific substrate. There was no functional difference between NAT1 alleles *4 and *10. In particular, there was no trend of increasing activity from NAT1*4/*4 to *4/*10 and *10/*10. Carriers of the NAT1 *11 and *14 alleles had a statistically significant lower enzyme activity compared with carriers of the *3, *4, or *10 alleles. Compared with the wild-type genotype NAT1*4/*4, activity of the NAT1*11/*11, NAT1*11/*10, and NAT1*11/*4 genotypes was reduced by 20.7%, 35.7%, and 31.5%, respectively. Activity of the NAT1*10/*14 and NAT1*4/*14 genotypes was reduced by 49.8% and 55.6%, respectively. The difference in NAT1 activity between the *4/*11 and *4/*14 genotypes was also significant (P < 0.01). The carrier of the NAT1*15/*15 genotype had no detectable enzyme activity. In conclusion, functional consequences of NAT1 mutations were tested in a large population. Activity in carriers of NAT1 alleles *3, *4, and *10 did not differ, alleles NAT1*11 and *14 appeared to be low activity alleles, and allele NAT1*15 had no activity.

4-Aminobenzoic Acid↗
PubMed2001

Inhibitory actions of luteolin on the growth and arylamine N-acetyltransferase activity in strains of Helicobacter pylori from ulcer patients.

Helicobacter pylori is now recognized as an important cause of type B gastritis, which is strongly associated with gastric and duodenal ulcer disease. H. pylori may be a causative factor in patients with gastric cancer. The growth inhibition and N-acetylation of 2-Aminofluorene (AF) or P-aminobenzoic acid (PABA) by arylamine N-acetyltransferase (NAT) in H. pylori were inhibited by luteolin, a component in herbal medicine. The growth inhibition was based on the changes of optical density (OD) by using a spectrophotometer. The N-acetylation of AF or PABA by NAT from H. pylori were assayed by the amounts of acetylated and non-acetylated AF or PABA in cytosols and intact bacteria of H. pylori by using HPLC. An inhibition of growth on H. pylori demonstrated that luteolin elicited a dose-dependent growth inhibition in the H. pylori cultures. Cytosols and suspensions of H. pylori with or without specific concentrations of luteolin co-treatment showed different percentages of AF or PABA acetylation. The data indicated that there was decreased NAT activity associated with increased levels of luteolin in H. pylori cytosols and suspensions. Using standard steady-state kinetic analysis, it was demonstrated that luteolin was a possible uncompetitive inhibitor to NAT enzyme in H. pylori. This report is the first demonstration to show that luteolin can inhibit H. pylori growth and NAT activity.

4-Aminobenzoic Acid↗
PubMedDate not supplied

[Effect of actipol on interferon level in tears (clinico-laboratory study)].

High interferon-inducing activity of a new antiviral drug actipol (0.007% para-aminobenzoic acid) instilled into the eye was demonstrated in animal experiments. In the present study the effect of actipol on interferon production in ocular tissues was investigated clinically. Interferon (IFN) content was measured in washings from the conjunctiva in 20 patients with herpetic keratitis, treated by actipol. Actipol was instilled frequently or injected subconjunctivally parabulbarly. The reference group consisted of 7 patients with herpetic keratitis treated with acyclovir locally. IFN titer was the last dilution of the sample ensuring 50% cell protection in comparison with complete cell destruction in the virus control. The samples were collected before, on days 1, 2, 3, 7 of treatment, and after clinical cure. Time course of IFN concentrations was wave-like in all the patients. The peak of IFN content surpassed the initial level 2-4-fold in all patients (26.13 +/- 5.9 vs. 58.9 +/- 4.4 U/ml, p < 0.01), which seems to be due to actipol induction of IFN production in the surface structures of the eyeball. In the reference group IFN content did not increase in comparison with the control during treatment. Hence, actipol induces the production of IFN in the surface eyeball structures in patients with various forms of herpetic keratitis.

4-Aminobenzoic Acid↗
PubMed1996

Longitudinal distribution of arylamine N-acetyltransferases in the intestine of the hamster, mouse, and rat. Evidence for multiplicity of N-acetyltransferases in the intestine.

Experimental and clinical evidence indicates that AcCoA:arylamine N-acetyltransferases (NATs; EC 2.3.1.5) are involved in the bioactivation and inactivation of a wide variety of arylamine, hydrazine, and carcinogenic arylamine xenobiotics. Longitudinal distribution of NATs in the intestine of the hamster, mouse, and two strains of rat was examined utilizing the model arylamine substrates procainamide(PA) and p-aminobenzoic acid (PABA) for the monomorphic (NAT1) and polymorphic (NAT2) enzymes in the rodent. NAT1 and NAT2 were distributed quite differently in each species examined. In particular, rat intestinal NATs were distributed equally throughout the intestinal tract. In contrast, hamster intestinal NATs decreased in activity from the proximal small intestine to the distal large intestine. Mouse NAT2 activity was highest in the cecum, whereas NAT1 was highest in the proximal small intestine. Although these model substrates have been shown to be selective for NATs, they are not specific. Therefore, a series of biochemical studies were undertaken to evaluate NAT multiplicity in the intestine of the F-344 rat. To assess multiplicity of NAT expression, selective inhibition, differential sensitivity to heat inactivation, and kinetic analysis were performed on intestinal cytosol. Eadie-Hofstee transformation of PA N-acetylation yielded a curvilinear plot indicative that a low affinity-high capacity enzyme aside from NAT1 (presumably NAT2) was contributing to PA N-acetylation activity. PA activity was found to exhibit approximately 4- to 5-fold greater thermostability than PABA activity. Furthermore, PA acetylation could be inhibited selectively with vinyl fluorenyl ketone (2.5 to 5 microM) but not with methotrexate (up to 2 mM). Taken together, these studies suggest the expression of both NAT1 and NAT2 in the intestine of the F-344 rat.

4-Aminobenzoic Acid↗
PubMed1992

p-aminobenzoate synthesis in Escherichia coli: kinetic and mechanistic characterization of the amidotransferase PabA.

p-Aminobenzoic acid (PABA) is an important precursor in the bacterial biosynthetic pathway for folate enzymes. This biosynthesis requires three separate proteins: PabA, PabB, and PabC. Together PabA and PabB convert glutamine and chorismate to glutamate and 4-amino-4-deoxychorismate. This aminochorismate is subsequently transformed to PABA by PabC. In this study, PabA from Escherichia coli has been purified to homogeneity from an overproducing construct and found to have no detectable glutaminase activity until addition of the E. coli PabB subunit. PabB forms a 1:1 complex with PabA to yield a glutaminase k(cat) of 17 min-1. The addition of chorismate, the substrate of PabB, induces a 2-fold increase of k(cat) as well as a 3-fold increase of Km for glutamine. The PabA/PabB complex has Kd less than 10(-8) M but does not form a stable complex isolable by gel filtration. Studies with the glutamine affinity label diazooxonorleucine (DON) reveal it is an inactivator of the glutaminase activity of the PabA/PabB complex, but DON does not alkylate and inactivate PabA alone. Similarly, while isolated PabA shows no tendency to form a glutamyl-enzyme intermediate, the PabA/PabB complex forms a covalent intermediate with [14C]glutamine on PabA that accumulates to 0.56 mol/mol in hydrolytic turnover. PabA is thus a conditional glutaminase, activated by 1:1 complexation with PabB.

4-Aminobenzoic Acid↗
PubMed2002

Candicidin biosynthesis in Streptomyces griseus.

The biosynthesis of the aromatic polyene macrolide antibiotic candicidin, produced by Streptomyces griseus IMRU 3570, begins with a p-aminobenzoic acid (PABA) molecule which is activated to PABA-CoA and used as starter for the head-to-tail condensation of four propionate and 14 acetate units to produce a polyketide molecule to which the deoxysugar mycosamine is attached. Using the gene coding for the PABA synthase ( pabAB) from S. griseusIMRU 3570 as the probe, a 205-kb region of continuous DNA from the S. griseus chromosome was isolated and partially sequenced. Some of the genes possibly involved in the biosynthesis of candicidin were identified including part of the modular polyketide synthase (PKS), genes for thioesterase, deoxysugar biosynthesis, modification, transport, and regulatory proteins. The regulatory mechanisms involved in the production of candicidin, such as phosphate regulation, were studied using internal probes for some of the genes involved in the biosynthesis of the three moieties of candicidin (PKS, aromatic moiety and amino sugar). mRNAs specific for these genes were detected only in the production medium (SPG) but not in the SPG medium supplemented with phosphate or in the inoculum medium, indicating that phosphate represses the expression of genes involved in candicidin biosynthesis. The modular architecture of the candicidin PKS and the availability of the PKSs involved in the biosynthesis of three polyene antibiotics (pimaricin, nystatin, and amphotericin B) shall make possible the creation of new, less toxic and more active polyene antibiotics through combinatorial biosynthesis and targeted mutagenesis.

4-Aminobenzoic Acid↗
PubMed1996

6,7-disubstituted 2,4-diaminopteridines: novel inhibitors of Pneumocystis carinii and Toxoplasma gondii dihydrofolate reductase.

Four novel, disubstituted diaminopteridines have been identified which antagonize the uptake of a folate precursor (para-aminobenzoic acid) by rat-derived Pneumocystis carinii maintained in short-term axenic culture at concentrations ranging from 4.5 to 26 microM. The compounds were at least 10 to 100 times more active than trimethoprim in this assay. None of these entities exhibited toxicity to mammalian cell lines at < 100 microM. The same structures also caused significant inhibition of Toxoplasma gondii tachyzoite replication within Madin-Darby bovine kidney cells at concentrations ranging from 0.1 to 10 microM. Three of the structures (GR92754, AH10639, and AH2504) were at least an order of magnitude more potent than the standard anti-T. gondii agent, pyrimethamine. All three entities were also significantly more potent and selective than pyrimethamine as inhibitors of T. gondii dihydrofolate reductase (DHFR), with 50% inhibitory concentrations within the range of 0.018 to 0.033 microM. One of these compounds, 6,7-dibutyl-2,4-diaminopteridine (GR92754), was also a potent and selective inhibitor of P. carinii DHFR (50% inhibitory concentration, 0.082 microM). GR92754 is the first DHFR inhibitor described that exhibits greater potency, selectivity, and intracellular activity against both organisms than any of the DHFR agents used clinically, namely, trimethoprim, pyrimethamine, and trimetrexate. This information could provide the starting point for examination of the pharmacokinetic and therapeutic potential of GR92754 and related chemical entities with animal models.

4-Aminobenzoic Acid↗
PubMedDate not supplied

Use of PABA test to check completeness of 24-h urine collections in elderly subjects.

The p-aminobenzoic acid (PABA) test has been successfully used as an indicator of completeness of 24-h urine collection in field studies of the general population. Our study was designed to investigate its validity for elderly people. Urinary excretion of fractionated oral doses of PABA was measured in 21 young control subjects (19-39 yr old) and 356 elderly (60-89 yr old) men and women. PABA excretion over 24 h was lower in elderly than in control subjects. Subjects aged greater than or equal to 70 yr had a lower recovery of the PABA dose than subjects aged 60-69 yr over the first 24 h, followed by a higher recovery over the next 24-48 h. The cumulative 48-h recovery was similar in all age classes of elderly subjects. However, 48% of the elderly subjects had a cumulative PABA recovery below the conventional cutoff for completeness (85%). These subjects also had consistently lower creatinine output and urinary volume. The lower 24-h urinary PABA recovery over 70 yr of age is interpreted to reflect the delayed renal clearance of the marker substance and indicates that the PABA test is unsuitable for this age group. The low 48-h cumulative recoveries found in all age classes of the elderly are thought to be caused by small unreported losses, which are recurrent in free-living populations.

4-Aminobenzoic Acid↗
PubMed1991

Effects of four chemicals on N-acetyltransferase activities in human U937 cell line.

The effects of p-aminobenzoic acid (PABA), procainamide (PA), anisidine (AN) and isoniazid (INH) on N-acetyltransferase (NAT) activities in cultured human cells were determined. PABA increased the specific activity of PABA NAT in the U937 cells but not in the Hep G2 cells. The enzyme activity in the PABA-treated U937 cells was restored to normal within 4 d after removing PABA from medium. These results imply that the PABA NAT activity in the U937 cells can be induced by PABA and the PABA NAT in the U937 cells is different from that in the Hep G2 cells. INH increased the INH NAT specific activity in the U937 cells but decreased the PABA NAT activity. AN decreased both the AN NAT and the PABA NAT specific activities in the U937 cells. PA did not affect the specific activities of PABA NAT or glucose-6-phosphate dihydrogenase (G-6-P DH) in the U937 cells. PABA also increased the specific activities of AN NAT and G-6-P DH. This implies that the induction effect of PABA on the PABA NAT activity is not specific. In this study the PABA NAT specific activity was increased only by PABA, and the INH NAT activity only by INH. However, the AN NAT activity could be induced by PABA but not by AN. These results indicate that induction of some but not all NAT activities has a limiting specificity.

4-Aminobenzoic Acid↗
PubMed1982

Mouse monoclonal antibodies to chicken VH idiotypic determinants reactivity with B and T cells.

We have prepared mouse monoclonal antibodies against idiotypic (Id) determinants on chicken antibodies to N-acetylglucosamine (NAGA) and p-aminobenzoic acid (PABA) made by inbred line EL 6(3) birds. The monoclonal anti-NAGA Id antibody, termed CId-1, reacted with affinity purified antibodies to NAGA, but not with antibodies specific for PABA, arsanilic acid (Ars), phosphorylcholine (PC), or with normal chicken IgG and IgM. The monoclonal anti-PABA ID antibody, termed CId-2, reacted with anti-PABA antibodies and to a lesser extent with anti-Ars antibodies, but not with anti-NAGA, anti-PC, and normal IgG and IgM. The Id determinants were found among antibodies to NAGA and PABA made by outbred and inbred lines of White Leghorn chickens. The binding of the CId-1 and CId-2 antibodies to intact homologous anti-NAGA and anti-PABA antibodies, respectively, was not hapten-inhibitable in either case. Both anti-Id antibodies reacted specifically with isolated homologous heavy chains, suggesting VH Id specificities. The monoclonal CId-1 and CId-2 antibodies were reactive by immunofluorescence with approximately 0.9 and 0.2%, respectively, of the circulating lymphocytes and with approximately 0.4 and 0.15 of plasma cells. CId-1+ and CId-2+ bursal cells were first detected on the 16th and 14th days of incubation, respectively; both reached maximal frequencies by the 17th day of incubation. The CId-2 antibody reacted exclusively with immunoglobulin-positive cells. The CId-1 antibody also reacted with a subpopulation (0.4%) of immunoglobulin-negative lymphocytes from normal and agammaglobulinemic chickens, and thus would appear to recognize an idiotypic determinant expressed by certain clones of B and T cells.

4-Aminobenzoic Acid↗
PubMed2001

High-performance liquid chromatographic determination of methyl anthranilate, hydroxymethylfurfural and related compounds in honey.

A high-performance liquid chromatographic method for determining 5-hydroxymethyl-2-furaldehyde (hydroxymethylfurfural), 2-furaldehyde (furfural), furan-2-carboxylic acid (2-furoic acid), furan-3-carboxylic acid (3-furoic acid), furan-3-carboxaldehyde (3-furaldehyde) and 2-aminobenzoic acid methyl ester (methyl anthranilate) in honey and honeydew samples is described. To prevent matrix interference and to isolate the compounds, a clean-up step which implies a solid-phase extraction on polymeric cartridges and an elution with 0.5 ml methanol is recommended. The compounds are separated on a reversed-phase column with a gradient of (A) 1% aqueous acetic acid-acetonitrile (97:3, v/v) and (B) acetonitrile-water (50:50, v/v), with UV detection at 250 nm. The method is applied to the analysis of samples from different botanical origin.

Calibration↗
PubMed2006

Specific inclusion mode of guest compounds in the amylose complex analyzed by solid state NMR spectroscopy.

The inclusion compound formation between linear amylose of molecular weight 102500 (AS100) and p-aminobenzoic acid (PA) during the sealed-heating process was investigated by powder X-ray diffractometry, infrared spectroscopy and solid state NMR spectroscopy. Sealed-heating of AS100 and PA at 100 degrees C for 6 h provided an inclusion compound with 6(1)-helix structure, while a 7(1)-helix structure was found when sealed-heating was carried out at 150 degrees C for 1 h. The formation of an inclusion compound was not observed when sealed-heating was performed at 50 degrees C for 6 h. The 7(1)-helix inclusion compound maintained its structure even during storage at high temperature while the 6(1)-helix inclusion compound decomposed and returned to the original V(a)-amylose upon heating to 180 degrees C. Quantitative determination revealed that one PA molecule could be included per one helical turn of AS100 for both 6(1)-helix and 7(1)-helix inclusion compounds. Solid state NMR spectroscopy suggested that PA molecules were included in the amylose helix core in the 7(1)-helix inclusion compound, while in the case of 6(1)-helix inclusion compound, PA molecules were accommodated in the interstices between amylose helices. Moreover, the inclusion compound formation by sealed-heating of AS100 was also observed when using PA analogues as guest compounds. The binding ratio of AS100 and PA analogues varied depending on the size of guest molecules.

4-Aminobenzoic Acid↗
PubMed1986

Identification and inheritance of inbred hamster N-acetyltransferase isozymes in peripheral blood.

Acetyl CoA-dependent p-aminobenzoic acid and p-aminosalicylic acid N-acetyltransferase (NAT) activity was determined in peripheral blood and blood cells from homozygous rapid (RR) acetylator (Bio. 87.20) and homozygous slow (rr) acetylator (Bio. 82.73/H) inbred hamsters and in their F1, F2 and backcross progeny. NAT activity was localized primarily in erythrocytes and was acetylator genotype dependent, as highest levels were expressed in homozygous rapid acetylator hamsters, intermediate levels in heterozygous acetylator hamsters and lowest levels in homozygous slow acetylator hamsters. Bio. 87.20 X Bio. 82.73/H F1 progeny expressed a unimodal nonoverlapping distribution of NAT activity intermediate between the RR and rr parentals. F2 generation progeny segregated into three modes (low, intermediate and high) of 21, 42 and 11, which is not significantly different from 1, 2 and 1. Bio. 82.73/H X F1 backcross progeny segregated into two modes (low and intermediate) of 18 and 16, whereas Bio. 87.20 X F1 backcross progeny segregated into two modes (intermediate and high) of 17 and 14, neither of which is significantly different from 1 and 1. These data are consistent with simple autosomal Mendelian inheritance of blood NAT activity by two codominant alleles at a single genetic locus. Partial purification of peripheral blood NAT activity by ion-exchange chromatography yielded separation of two isozymes that both exhibited acetylator genotype-dependent expression with highest activity in RR, intermediate activity in Rr and nondetectable activity in rr genotypes, respectively.

4-Aminobenzoic Acid↗