Search PubMed⌕ Search

Biomedical subjects

R Chatterjee

Publications and source records attributed to R Chatterjee.

At least 37 records · Page 2Linked to original sources
PubMed2000

Reversible hypogonadotrophic hypogonadism in sexually infantile male thalassaemic patients with transfusional iron overload.

OBJECTIVE: To determine the severity and reversibility of the lesion in the hypothalamic-pituitary (H-P) axis of male transfusion-dependent thalassaemic patients with failed puberty (FP). DESIGN AND SUBJECTS: The hypothalamic-pituitary axes of 20 male thalassaemic patients (study group) were compared with two male subjects with idiopathic hypogonadotrophic hypogonadism (IHH) and five prepubertal healthy siblings (control group). GnRH-gonadotrophin insufficiency was characterized by nocturnal 12 h ultradian gonadotrophin profiles followed by a 100 microg GnRH bolus test (GBT) 4-6 times at 6 monthly intervals. Thalassaemic and IHH patients were then subjected to pulsatile subcutaneous GnRH infusions every 120 minutes for 3 months. Ultradian gonadotrophin profiles and GBT were repeated after 6 weeks of GnRH infusion and again at 3 months following infusion. MEASUREMENTS: FSH and LH were measured by radio-immunoassay. Ferritin was assayed by an immunoradiometric method. RESULTS: Patients with IHH who were apulsatile prior to infusion, developed normal gonadotrophin pulses with marked increment in their gonadotrophin responses to the GBT after 3 months of GnRH infusion. In contrast, the thalassaemic patients with apulsatile failed puberty (AFP) remained apulsatile (nonresponders) and had no increment in their gonadotrophin responses to the GBT after GnRH infusion. All patients with pulsatile failed puberty (PFP) had abnormal gonadotrophin pulses prior to GnRH infusion. Their pulse defects were either totally or partially corrected (responders) following infusion. The serum ferritin levels (9500 +/- 500 microg/l vs. 5966.67 +/- 1139 microg/l; P < 0.01) and percentage of organ dysfunction (87% vs. 17%; P < 0.01) were higher in the nonresponders than the responders. CONCLUSIONS: This study shows that thalassaemic patients with severe organ damage and iron overload are likely to be apulsatile with irreversible damage to their hypothalamo-pituitary axis, while those with less severe iron overload are likely to have potentially reversible hypogonadotrophic hypogonadism (HH). Our results also suggest that gonadotrophin pulse parameters, rather than the gonadotrophin response to a GnRH bolus following prolonged pulsatile GnRH infusion, may be more useful in discriminating reversible from irreversible hypogonadotrophic hypogonadism.

Adolescent↗
PubMed2000

Testicular and sperm DNA damage after treatment with fludarabine for chronic lymphocytic leukaemia.

This study investigated whether chemotherapy using fludarabine (FLU) caused testicular damage and if cytotoxicity could be detected as sperm DNA damage in the single cell Comet assay. A patient with chronic lymphocytic leukaemia requesting preservation of fertility was treated with seven monthly cycles of fludarabine (45.8 mg total dose per cycle). Testicular assessments, serum follicle stimulating hormone (FSH), luteinizing hormone (LH), and testosterone measurements, semen analysis and sperm Comet assays were carried out at presentation (pre-FLU therapy), after 1 and 7 months of FLU treatment, and finally at 11 months after completion of chemotherapy. We found that testicular damage occurred within a month, as indicated by reduced testicular volume, oligozoospermia, elevated FSH and LH, and lower testosterone concentrations. Spermatozoa with a large range of DNA damage were detected in the samples from both the control and treated men. DNA damage in the spermatozoa was marked by 7 months of FLU treatment. The high levels of sperm DNA damage seen during and possibly persisting after treatment suggests that caution should be exercised if the ejaculates from these men are used for in-vitro fertility treatment. Further experiments are needed to assess the biological significance of these DNA changes; it may, however, be prudent at present to be cautious when counselling these patients.

Antineoplastic Agents↗
PubMed2000

Testicular tissue cryopreservation in boys. Ethical and legal issues: case report.

Sperm preservation prior to chemotherapy and radiotherapy is common practice in adult males. Spermatozoa are usually retrieved from an ejaculated sample although there are occasions when testicular tissue is used as the source. These techniques of sperm preservation present minimal ethical objections as the patients give their informed consent. Sperm preservation in children presents practical and ethical dilemmas in that the children cannot always give their informed consent, there are no regulatory guidelines and there is no guarantee that spermatogenesis is occurring. With the rapid advances in reproductive technology and the possible future use of immature germ cells by in-vitro maturation or transplantation, the demand for immature testicular tissue preservation is likely to increase. More information for the parents and oncologists with regard to this subject is needed to allow informed decisions to be made on behalf of the children. These issues are discussed using two cases of children having testicular tissue preservation.

Adolescent↗
PubMed2000

p107 is active in the nucleolus in non-dividing human granulosa lutein cells.

Cells are maintained in a quiescent state by members of the retinoblastoma protein family, pRb and p130. Both are phosphoproteins and hypophosphorylated forms of pRb and p130 bind and repress the activity of E2F transcription factors, thereby preventing entry into the cell cycle. Mitogenic stimulation causes activation of cyclin dependent kinases (cdk) that phosphorylate both pRb and p130, thereby releasing E2F factors which stimulate the transcription of a number of genes that are required for DNA synthesis and for regulating the cell cycle. In non-dividing cells, cdks are maintained in an inactive state by cdk inhibitor proteins such as p27(Kip1). The aim of our study was to determine how E2F complexes are regulated during the differentiation of human primary granulosa lutein cells (GLC) of the corpus luteum (CL). The CL is formed in the ovary after ovulation at the terminal stage of folliculogenesis after completion of maturation and differentiation of Graafian follicles. As shown by flow cytometry GLC are not dividing, being predominantly in the G(0)/G(1) phase of the cell cycle and, consistent with this, they contain the cdk inhibitor protein, p27(Kip1), but not E2F-1 which is normally expressed only in proliferating cells. The GLC do express E2F-4, hypophosphorylated pRb, p130 forms 1 and 2 and, surprisingly, hypophosphorylated p107. p107 is normally present only in dividing cells where it regulates E2F activity during the cell cycle. These forms of pRb, p130 as well as p107, together with E2F-4 are all active in that they can bind an E2F DNA-binding site in a pull-down assay. Immunocytochemistry shows that these proteins are expressed in almost all GLC but have different sub-cellular distribution: p107 is concentrated in nucleoli, while p130 and E2F-4 show relatively even nuclear and cytoplasmic distributions. Both pRb and p130 have been implicated previously in repressing E2F activity in many different cell types during cell cycle arrest in G(0)/G(1). We conclude that p107 is active in human primary GLC but its nucleolar localisation would suggest that it represses ribosomal RNA synthesis rather than E2F activity.

Cell Cycle↗
PubMed1999

Requirement of NifX and other nif proteins for in vitro biosynthesis of the iron-molybdenum cofactor of nitrogenase.

The iron-molybdenum cofactor (FeMo-co) of nitrogenase contains molybdenum, iron, sulfur, and homocitrate in a ratio of 1:7:9:1. In vitro synthesis of FeMo-co has been established, and the reaction requires an ATP-regenerating system, dithionite, molybdate, homocitrate, and at least NifB-co (the metabolic product of NifB), NifNE, and dinitrogenase reductase (NifH). The typical in vitro FeMo-co synthesis reaction involves mixing extracts from two different mutant strains of Azotobacter vinelandii defective in the biosynthesis of cofactor or an extract of a mutant strain complemented with the purified missing component. Surprisingly, the in vitro synthesis of FeMo-co with only purified components failed to generate significant FeMo-co, suggesting the requirement for one or more other components. Complementation of these assays with extracts of various mutant strains demonstrated that NifX has a role in synthesis of FeMo-co. In vitro synthesis of FeMo-co with purified components is stimulated approximately threefold by purified NifX. Complementation of these assays with extracts of A. vinelandii DJ42. 48 (DeltanifENX DeltavnfE) results in a 12- to 15-fold stimulation of in vitro FeMo-co synthesis activity. These data also demonstrate that apart from the NifX some other component(s) is required for the cofactor synthesis. The in vitro synthesis of FeMo-co with purified components has allowed the detection, purification, and identification of an additional component(s) required for the synthesis of cofactor.

Azotobacter vinelandii↗
PubMed1998

Ejection of neutral molecules from ion-bombarded organic surfaces.

Time-of-flight distributions of neutral molecules ejected from various organic surfaces have been measured subsequent to 8 keV Ar+ and H2+ ion bombardment. The distributions show that depending on the physical and chemical nature of the substrate, the neutral molecules have strikingly different desorption profiles. For C6H6/Ag¿111¿, at low coverage the C6H6 molecules eject with energies in the range 0.25-1 eV while at high coverage most of the molecules desorb with thermal kinetic energies (approximately 0.04 eV). At intermediate coverage two peaks are present in the time-of-flight distribution indicating that two different mechanisms contribute to the desorption process. For self-assembled monolayers of phenylethanethiol on Au, while a minor ejection is observed at higher kinetic energy (approximately 1 eV) most of the molecules desorb with thermal kinetic energies (approximately 0.03 eV). Pyrenebutyric acid molecules ejected from monolayer and multilayer samples have kinetic energies close to 0.2 eV. One ejection mechanism is observed in this case. For tryptophan, most molecules eject with kinetic energies close to 0.1 eV. In addition, a feature unique to this case is the continuous emission of molecules from the surface that extends beyond 200 microseconds after ion impact. For all the multilayer samples investigated, a molecular collision cascade in the solid leads to ejection of molecules with kinetic energies in the range 0.1-0.3 eV.

Energy Transfer↗
PubMed1998

Correlation between human papillomavirus DNA detection in maternal cervical smears and buccal swabs of infants.

Acquisition of human papillomavirus (HPV) infection in buccal mucosa by the infants at birth has been investigated. Presence of HPV DNA was evaluated in cervical smears of 30 pregnant women before delivery and in buccal swabs of the corresponding 31 infants (1 set of twins). HPV DNA was detected among the 40% of women, 16% of infants an the detection was concordant in 23 mother-infant pairs. HPV DNA was demonstrated in buccal mucosal cells of 41.6% of the infants born to HPV positive mothers. Maternal-infant transmission was highest for HPV 6/11. Assessment of the risk of developing HPV related oral lesions in children at later life owing to acquisition of HPV during perinatal period may help in determining a strategy to combat the disease.

Cheek↗
PubMed1997

In vitro synthesis of the iron-molybdenum cofactor and maturation of the nif-encoded apodinitrogenase. Effect of substitution of VNFH for NIFH.

NIFH (the nifH gene product) has several functions in the nitrogenase enzyme system. In addition to reducing dinitrogenase during nitrogenase turnover, NIFH functions in the biosynthesis of the iron-molybdenum cofactor (FeMo-co), and in the processing of alpha2beta2 apodinitrogenase 1 (a catalytically inactive form of dinitrogenase 1 that lacks the FeMo-co) to the FeMo-co-activatable alpha2beta2gamma2 form. The molybdenum-independent nitrogenase 2 (vnf-encoded) has a distinct dinitrogenase reductase protein, VNFH. We investigated the ability of VNFH to function in the in vitro biosynthesis of FeMo-co and in the maturation of apodinitrogenase 1. VNFH can replace NIFH in both the biosynthesis of FeMo-co and in the maturation of apodinitrogenase 1. These results suggest that the dinitrogenase reductase proteins do not specify the heterometal incorporated into the cofactors of the respective nitrogenase enzymes. The specificity for the incorporation of molybdenum into FeMo-co was also examined using the in vitro FeMo-co synthesis assay system.

Apoproteins↗
PubMed1997

Activation of parietal cell by mercaptomethylimidazole: a novel inducer of gastric acid secretion.

Mercaptomethylimidazole (2-Mercapto-1-methylimidazole, MMI), an antithyroid drug of thionamide group, significantly activated the parietal cell for acid secretion, as evidenced by increased O2 consumption by more than 2.5-fold over the basal level. When compared, MMI-induced activation was similar to that of histamine but significantly higher than that of isobutylmethylxanthine or carbachol. Activation by MMI was not prevented by receptor blockers of the parietal cell, indicating that its effect was not mediated through the cell surface histamine-H2 receptor or the muscarinic receptor. However, the activation was almost completely blocked only by omeprazole, an established inhibitor of the terminal proton-pumping H+-K+-ATPase of the parietal cell. That MMI-induced activation was coupled with the H+ transport was further confirmed by significant increase in [14C]-aminopyrine uptake by MMI in rabbit gastric gland preparation. MMI-dependent activation of the parietal cell correlated well with the inhibition of the endogenous peroxidase activity. In vitro studies indicated that MMI irreversibly inactivated both peroxidase and catalase activity of the parietal cell in presence of H2O2. As inactivation of these H2O2-scavenging enzymes should increase accumulation of intracellular H2O2, the effect of latter was studied on acid secretion. H2O2 at a low concentration, stimulated acid secretion by sevenfold in isolated gastric mucosa, which was sensitive to omeprazole. It also significantly stimulated [14C]-aminopyrine uptake in gastric gland preparation. We suggest that MMI activated parietal cells to stimulate acid secretion by endogenous accumulation of H2O2 through inactivation of the peroxidase-catalase system.

Aminopyrine↗
PubMed1997

Mechanism-based inactivation of lacrimal-gland peroxidase by phenylhydrazine: a suicidal substrate to probe the active site.

Humans are exposed to various hydrazine derivatives for therapeutic control of several diseases, and mammalian peroxidases are implicated in the oxidative metabolism of many drugs. The results presented here indicate that lacrimal-gland peroxidase is irreversibly inactivated in a mechanism-based way by phenylhydrazine, which acts as a suicidal substrate in the presence of H2O2. The pseudo-first-order kinetic constants for inactivation at pH 5.5 are Ki=18 microM, kinact=0.25 min-1 and tau50=2.75 min, with a second-order rate constant of 0.75x10(4) M-1.min-1. Approx. 27 mol of phenylhydrazine and 54 mol of H2O2 are required per mol of enzyme for complete inactivation. The pH-dependent inactivation kinetics indicate the involvement of an ionizable group on the enzyme with a pKa value of 5.4, protonation of which favours inactivation. SCN-, the plausible physiological electron donor of the enzyme, protects it from inactivation. Binding studies by optical difference spectroscopy indicate that phenylhydrazine interacts with the enzyme with a KD value of 60 microM, and its binding is prevented by the presence of SCN-. The enzyme is also protected by 5, 5-dimethyl-1-pyrroline N-oxide, a free-radical trap, suggesting the involvement of a radical species in the inactivation. ESR studies indicate the formation of a spin-trapped phenyl radical (aN=15.9G and abetaH=24.8G) generated on incubation of phenylhydrazine with the enzyme and H2O2. A 75% loss of the Soret spectrum is observed when the enzyme is completely inactivated. However, in the presence of the spin trap, spectral loss is prevented and the enzyme compound II is readily reduced to the native state by phenylhydrazine. The phenylhydrazine-inactivated enzyme reacts with H2O2 or CN- to form compound II or the cyanide complex with a characteristic spectrum, indicating that haem iron is protected from attack by the radical species. The inactivated enzyme binds SCN- with a KD value similar to that of the native enzyme (15+/-3 mM), suggesting that the donor-binding site remains unaffected. CD studies of the inactive enzyme show complete disappearance of the Soret band at 409 nm with the appearance of a new band at 275 nm. This indicates that the haem environment of the enzyme is perturbed in the inactive form. As benzene, the end product of phenylhydrazine oxidation, has no effect on the enzyme, we suggest that the phenyl radical formed by one-electron oxidation by catalytically active enzyme inactivates it by incorporation in the vicinity of its haem moiety. The data support the use of phenylhydrazine as a probe for structural and mechanistic analysis of the active site of the lacrimal-gland peroxidase.

Animals↗
PubMed1997

Characterization of VNFG, the delta subunit of the vnf-encoded apodinitrogenase from Azotobacter vinelandii. Implications for its role in the formation of functional dinitrogenase 2.

The vnf-encoded apodinitrogenase (apodinitrogenase 2) from Azotobacter vinelandii is an alpha2beta2delta2 hexamer. The delta subunit (the VNFG protein) has been characterized in order to further delineate its function in the nitrogenase 2 enzyme system. Two species of VNFG were observed in cell-free extracts resolved on anoxic native gels; one is composed of VNFG associated with the VNFDK polypeptides, and the other is a homodimer of the VNFG protein. Both species of VNFG are observed in extracts of A. vinelandii strains that accumulate dinitrogenase 2, whereas extracts of strains impaired in the biosynthetic pathway of the iron-vanadium cofactor (FeV-co) that accumulate apodinitrogenase 2 (a catalytically inactive form of dinitrogenase 2 that lacks FeV-co) exhibit only the VNFG dimer on native gels. FeV-co and nucleotide are required for the stable association of VNFG with the VNFDK polypeptides; this stable association can be correlated with the formation of active dinitrogenase 2. The iron-molybdenum cofactor was unable to replace FeV-co in promoting the stable association of VNFG with VNFDK. FeV-co specifically associates with the VNFG dimer in vitro to form a complex of unknown stoichiometry; combination of this VNFG-FeV-co species with apodinitrogenase 2 results in its reconstitution to dinitrogenase 2. The results presented here suggest that VNFG is required for processing apodinitrogenase 2 to functional dinitrogenase 2.

Animals↗
PubMed1997

Evaluation of argyrophilic nucleolar organizer regions (AgNORs) in oral carcinomas in relation to human papillomavirus infection and cytokinetics.

The numbers of argyrophilic nucleolar organizer regions (AgNORs) were quantified in oral carcinomas (n = 39) with or without human papillomavirus (HPV) infection. The AgNOR counts of the HPV-positive samples (7.15 +/- 2.13) were not significantly (P = 0.09) higher than those of the HPV-negative ones (6.16 +/- 1.89). Furthermore, the lesions infected with multiple HPV types had greater counts than those with HPV type 16/18 infection alone. Significant differences were observed between the mean counts of the poorly (10.50 +/- 0.54), moderately (7.31 +/- 1.07) and well- (5.12 +/- 0.85) differentiated carcinomas. The mean AgNOR numbers in the oral carcinomas at TNM stages III/IV were found to be significantly (P < 0.01) higher than the numbers in corresponding stage II lesions. Cytokinetics of the lesions assessed by the bromodeoxyuridine (Brdu) labelling index (LI%) showed a linear correlation (r = 0.91; P < 0.0001) with their respective mean AgNOR counts.

Adult↗
PubMed1997

African strains of hepatitis E virus that are distinct from Asian strains.

Partial genomic sequences of four hepatitis E virus (HEV) strains from Africa (Morocco and Tunisia) and one from Central Asia (Tashkent, Uzbekistan) were obtained. The reverse transcriptase-polymerase chain reaction was used to amplify 5' and hypervariable regions of open reading frame 1 (ORF1) and a region overlapping all 3 ORFs. Sequence analysis of these regions revealed the African strains to be quite distinct from all known Asian strains but more similar to them than to the Mexican strain. Sequence analysis of the Tashkent strain revealed almost complete identity with another central Asian strain from Osh, Kirgizia. These results thus further confirm the geographical origin of HEV strain divergence.

Animals↗
PubMed1997

Longitudinal study of human milk creamatocrit and weight gain in exclusively breastfed infants.

OBJECTIVE: To determine the creamatocrit values of breastmilk at different lactational periods during the first 6 months after delivery and its relation to infant growth. DESIGN: Prospective follow-up study. SETTING: Maternity and well baby clinics of a metropolitan teaching, a rural teaching and a suburban municipal hospital. SUBJECTS: 1322 exclusively breastfed infants and their mothers. There were 160 preterm, 281 term low birth weight (LBW) and 881 term appropriate for date (AFD) babies. METHODS: Creamatocrit of breastmilk and infant's body weight were recorded at 4,8,12,16,20 and 24 weeks after birth. RESULTS: Creamatocrit values of breastmilk in all mothers increased upto 16 post partum weeks and then declined. There were no significant differences in creamatocrit values of breastmilk of mothers of preterm, term LBW and term non-LBW infants. Preterm and term LBW infants showed a catch up in body weight with the term AFD group by 20 weeks post-partum. CONCLUSIONS: The breastmilk creamatocrit progressively rises upto the fourth month of lactation but is not influenced by gestation or intra uterine growth retardation. There is no relationship between breastmilk creamatocrit and infant growth. Exclusive breast feeding adequately supports growth of LBW infants in comparison to their normal peers during the first 6 months of life.

Body Weight↗
PubMed1996

Lactoperoxidase-catalysed oxidation of indomethacin, a nonsteroidal antiinflammatory drug, through the formation of a free radical.

Lactoperoxidase (LPO, EC 1.11.1.7; donor-H2O2 oxidoreductase) catalyses the oxidation of indomethacin, a nonsteroidal antiinflammatory drug by H2O2 as measured by time-dependent decay of indo-methacin extinction at 280 nm and concurrent appearance of stable oxidation product(s) at 412 nm. From a plot of log Vmax against varying pH of indomethacin oxidation, involvement of an ionizable group of the enzyme having pka = 5.7 could be ascertained for controlling the oxidation process. Spectral studies revealed that LPO-compound II oxidises indomethacin through one-electron transfer and is reduced to the native ferric state as shown by its spectral shift from 430 nm to 412 nm through an isosbestic point at 421 nm. The one-electron oxidation product is a nitrogen-centered free radical detected as a 5,5-dimethyl-l-pyrroline N-oxide (DMPO) adduct (alpha N = 15 G, alpha H beta = 16 G) in electron spin resonance spectroscopy. The free radical is scavenged by reaction with O2 as shown by O2 consumption sensitive to the free-radical trap, DMPO. Binding studies by optical difference spectroscopy indicate that indomethacin binds to LPO with an apparent KD value of 24.5 microM. The free energy change, delta G', for the binding is -26.3 KJ mol-1, suggesting that the interaction is favourable for oxidation. Indomethacin binding remains unaltered by a change of pH from 5.25 to 7.5, presumably because of hydrophobic interaction. The binding is competitive with resorcinol, an aromatic electron donor, showing the KD value to be as high as 100 microM. We suggest that indomethacin interacts at the aromatic donor binding site and is oxidised by one-electron transfer by LPO catalytic intermediates to stable oxidation product(s) through the formation of a free radical.

Animals↗
PubMed1996

Purification and characterization of the vnf-encoded apodinitrogenase from Azotobacter vinelandii.

The vnf-encoded apodinitrogenase (apodinitrogenase 2) has been purified from Azotobacter vinelandii strain CA117.30 (DeltanifKDB), and is an alpha2beta2delta2 hexamer. Apodinitrogenase 2 can be activated in vitro by the addition of the iron-vanadium cofactor (FeV-co) to form holodinitrogenase 2, which functions in C2H2, H+, and N2 reduction. Under certain conditions, the alpha2beta2delta2 hexamer dissociates to yield the free delta subunit (the VNFG protein) and a form of apodinitrogenase 2 that exhibits no C2H2, H+, or N2 reduction activities in the in vitro FeV-co activation assay; however, these activities can be restored upon addition of VNFG to the FeV-co activation assay system. No other vnf-, nif-, or non-nif-encoded proteins were able to replace the function of VNFG in the in vitro processing of alpha2beta2 apodinitrogenase 2 (in the presence of FeV-co) to a form capable of substrate reduction. Apodinitrogenase 2 is also activable in vitro by the iron-molybdenum cofactor to form a hybrid enzyme with unique properties, most notably the inability to reduce N2 and insensitivity to CO inhibition of C2H2 reduction.

Azotobacter vinelandii↗
PubMed1996

Characterization of sheep lacrimal-gland peroxidase and its major physiological electron donor.

A soluble sheep lacrimal-gland peroxidase was purified to apparent homogeneity. It had a native molecular mass of 75 kDa with a subunit molecular mass of 82 kDa and an isoelectric point of 6.5. Western blotting showed that it shares some of the enzyme antigenic determinants in common with other soluble peroxidases. The enzyme exhibits a Soret peak at 410 nm which is shifted to 431 nm by 5 equiv. of H2O2 due to the formation of compound II. The latter is, however, unstable and gradually returns to the native state. The enzyme forms complexes with CN- and N3- and is reduced by dithionite showing a characteristic reduced peroxidase spectrum. Although the enzyme oxidizes I-, SCN- and Br- optimally at pH 5.5., 5.25 and 5.0 respectively, at physiological pH, it oxidizes I- and SCN- only. Since extracellular SCN- concentration is much higher than I-, SCN- may act as the major electron donor to the enzyme. The second-order rate constants for the reaction of the enzyme with H2O2 (k+1) and of compound I with SCN- (k+2) were 4 X 10(7) M-1 X s-1 and 8.1 X 10(5) M-1 X s-1 respectively. A plot of log Vmax against pH yields a sigmoidal curve consistent with a single ionizable group on the enzyme with a pK(a) value of 5.75, controlling thiocyanate oxidation. In a coupled system with the peroxidase, H2O2, SCN-, GSH, NADPH and glutathione reductase, peroxidase-catalysed SCN- oxidation by H2O2 could be coupled to NADPH consumption. The system is proposed to operate in vivo for the efficient elimination of endogenous H2O2.

Animals↗