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PubMed1991

Evaluation of the ability of the angiotensin-converting enzyme inhibitor captopril to scavenge reactive oxygen species.

Captopril, an inhibitor of angiotensin-converting enzyme, has been suggested to have additional cardioprotective action because of its ability to act as an antioxidant. The rates of reaction of captopril with several biologically-relevant reactive oxygen species were determined. Captopril reacts slowly, if at all, with superoxide (rate constant less than 10(3) M-1 s-1) or hydrogen peroxide (rate constant less than M-1 s-1). It does not inhibit peroxidation of lipids stimulated by iron ions and ascorbate or by the myoglobin/H2O2 system. Indeed, mixtures of ferric ion and captopril can stimulate lipid peroxidation. Captopril reacts rapidly with hydroxyl radical (rate constant greater than 10(9) M-1 s-1) but might be unlikely to compete with most biological molecules for OH because of the low concentration of captopril that can be achieved in vivo during therapeutic use. Captopril did not significantly inhibit iron ion-dependent generation of hydroxyl radicals from hydrogen peroxide. By contrast, captopril is a powerful scavenger of hypochlorous acid: it was able to protect alpha 1-antiproteinase (alpha 1 AP) against inactivation by this species and to prevent formation of chloramines from taurine. We suggest that the antioxidant action of captopril in vivo is likely to be limited, and may be restricted to protection against damage by hypochlorous acid derived from the action of neutrophil myeloperoxidase.

Animals↗

PubMed1981

The influence of effectors on the refolding (reactivation) of immobilized trypsin.

The refolding of immobilized trypsin in the presence of various effectors of its enzymatic activity has been studied. Trypsin covalently bound to Sephadex G-200 was made to unfold in a concentrated solution of urea; at the same time its S-S bonds were split with the help of dithiothreitol. The preparation was then separated from the splitting agents, and one of the effectors of the enzymatic activity of trypsin (boric acid, benzamidine, pancreatic or soybean inhibitors of trypsin, N-benzoyl-L-arginine ethyl ester, and N-tosyl-L-arginine methyl ester) was added and the reactivation of immobilized enzyme was studied in the absence of catalysts of thiol-disulphide exchange. The following effects were found. 1. The reactivation of immobilized trypsin in the presence of specific substrates or protein inhibitors proceeds with the same yield (2-5%) as in their absence. 2. In the presence of benzamidine or boric acid (competitive inhibitors) the reactivation yields of the immobilized trypsin increased 5-fold and 12-fold respectively, and became equal to 15% and 40%. Comparison of these results with the statistical probability of formation of the six native S-S bonds from twelve SH groups (approximately 0.01%) shows that if trypsin is made to refold in an immobilized state in the presence of a 'good' effector, the yield of the reactivation of the enzyme can be increased several thousand times. 3. Similar effects were observed for trypsin immobilized on Sepharose 4B. A model is suggested in terms of which the influence of various effectors on trypsin refolding is explained as being a result of their ability to bind with an intermediate folded forms of protein followed by a shift of the equilibrium towards 'regular' conformers.

Catalysis↗

PubMed1982

Red cell enzyme activity during blood storage and reactivation of phosphofructokinase.

Activities of 21 red cell enzymes were measured in 15 units of CPD-Al anticoagulated blood before and after 35 days of storage. Paired t-tests revealed that five of the enzyme activities decreased significantly after 35 days of storage (P less than 0.05) while four increased significantly after storage (P less than 0.05). The most striking change was in phosphofructokinase (PFK), which decreased an average of 33% (P less than 0.005). Mean lactate dehydrogenase activity increased to 128% of its zero-day activity (P less than 0.005). Percent red cell survival, determined by reinfusion of a 51Cr-tagged aliquot of stored blood into the autologous donor, was highly correlated with 35-day ATP levels (r = 0.97; P less than 0.001). No significant relationships between two measures of red cell survival and any of the nine significantly altered enzymes were found. Studies of reactivation of PFK in hemolysates using 4 mM concentrations of numerous compounds indicate that the compounds or combinations of compounds used which reactivate PFK significantly all contain at least one high-energy phosphate group. These data suggest that loss of PFK activity during storage may be due to loss of organic phosphates. Whether the changes described have an important role in blood transfusion remains to be determined.

Adenosine Triphosphate↗

PubMed2006

Increased C reactive protein and cardiac enzyme levels after coronary stent implantation. Is there protection by remote ischaemic preconditioning?

AIM: To investigate whether remote ischaemic preconditioning (RIPC) can attenuate the inflammatory response and enzyme leakage that can occur after uncomplicated routine percutaneous coronary intervention (PCI). METHODS: 41 consecutive normotensive patients with stable angina and single-vessel disease were assigned to be exposed to RIPC (n = 20) or not (control group; n = 21) before elective PCI with stent implantation. RIPC was induced by three cycles of 5-min ischaemia-reperfusion of both upper limbs (inflation/deflation of blood pressure cuff). C reactive protein (CRP), creatine phosphokinase (CK), CK cardiac isoenzyme (CK-MB) and troponin I (TNI) were serially measured for 48 h. RESULTS: No difference in baseline values was observed between the groups. The CRP rose significantly (p<0.001) and at 48 h was similarly increased (>fourfold) in both groups (15.7 (2.6) v 14.0 (3.3) mg/l, RIPC v control; p = NS). However, sub-group analysis on the basis of statin use showed that the highest rise was in the group of patients with RIPC not taking statins and was significantly greater than in patients with RIPC taking statins (23.8 (3.71) v 11.4 (3.0) mg/l, respectively, p<0.01). Both CK-MB and TNI leakage were raised (slightly but significantly) after PCI in controls at 24 h compared with baseline values. However, this small rise was significantly worse after RIPC (CK-MB, 1.33 (0.27) v 3.57 (0.97) ng/ml, p<0.01; TNI, 0.255 (0.059) v 0.804 (0.232) ng/ml, p<0.05, respectively at 24 h). The increase was more marked in the RIPC subgroup not taking statins. CONCLUSIONS: RIPC does not reduce, but exacerbates, the enzyme and TNI release from the heart after single-vessel angioplasty with stent. Furthermore, the increased circulating CRP remains raised. It seems that there is an enhanced inflammatory response after RIPC in the absence of statin treatment.

Angina Pectoris↗

PubMed1993

Modulation of the fumarases of Escherichia coli in response to oxidative stress.

The [4Fe-4S]-containing fumarases A + B of Escherichia coli are susceptible to oxidative inactivation, while fumarase C, which is not an iron-sulfur protein, is induced under oxidative conditions. Thus, imposition of oxidative stress, whether by addition of paraquat or by mutational deletion of superoxide dismutases, diminished fumarases A + B while elevating fumarase C. H2O2 appeared to be one cause of the inactivation of fumarases A + B, but was not involved in the induction of fumarase C. Thus lack of hydroperoxidases I and II did increase the paraquat-elicited inactivation of fumarases A + B without affecting the induction of fumarase C by paraquat. The importance of Fe(II) for the unstable fumarases was exposed by alpha,alpha'-dipyridyl, which decreased fumarases A + B without affecting fumarase C or the inductive effect thereon of paraquat. The oxidative inactivation and the subsequent reactivation of fumarase A was examined in extracts. Under air there was a first-order inactivation of fumarase A, which was rapidly reversed when O2 was excluded. The role of iron loss and restitution, in this inactivation and reactivation, was clarified by EDTA, which was without effect on the aerobic inactivation, but blocked the anaerobic reactivation. These results are consistent with a predominantly ferric state of the available iron in the presence of O2 and of the ferrous state in the absence of O2.

2,2'-Dipyridyl↗

PubMed1986

Activation and active sites of nickel-containing hydrogenases.

Hydrogenases that contain nickel and iron-sulphur clusters also have a regulatory mechanism, by which exposure to oxidants such as oxygen prevents their reaction with hydrogen. Treatment with reducing agents then causes reactivation. In some hydrogenases from Desulfovibrio species, there is evidence that there are at least two different deactivated states, which differ in their rates of reductive reactivation. The membrane-bound hydrogenase of D. desulfuricans, Norway strain, the periplasmic hydrogenase of D. gigas and the membrane-bound hydrogenase of Alcaligenes eutrophus can be isolated in a state (termed "Unready") which requires up to several hours for full activation by hydrogen. By contrast the soluble hydrogenases of D. desulfuricans and A. eutrophus can be reactivated relatively rapidly. In all of these enzymes, with the exception of the latter one, the existence of the activated and deactivated states can be correlated with different ESR-detectable forms of nickel. The possible functions of nickel and [Fe-4S] clusters in catalysis are discussed.

Alcaligenes↗

PubMed1987

Phosphodiesterase I in human urine: purification and characterization of the enzyme.

Phosphodiesterase I [EC 3.1.4.1] was purified from normal human urine in a highly purified state free from phosphodiesterase II, RNase, DNase I, DNase II, and phosphatase by column chromatographies of DEAE-Toyopearl, butyl-Toyopearl, Affi-Gel blue, and Sephadex G-150. The molecular weight of the enzyme was 1.9 x 10(5) and the pH optimum around 9.0 with p-nitrophenyl deoxythymidine 5'-phosphate as the substrate. The enzyme hydrolyzed the 3'-5' linkage of various dinucleoside monophosphates at approximately the same rate and the phosphodiester bonds of cyclic 3',5'-mononucleotides to produce mononucleoside 5'-phosphate. The enzyme also hydrolyzed ADP to 5'-AMP and Pi, ATP to 5'-AMP and PPi, and NAD+ to 5'-AMP and NMN. The enzyme activity was abolished by removal of metal ions with EDTA, and the metal-free enzyme was reactivated on the addition of Zn2+. The enzyme activity was also abolished by some reducing agents and the inhibition was reversed by Zn2+. The metal-free enzyme was less stable than the native enzyme, and Zn2+ and Co2+ restored the stability of the metal-free enzyme to the level of the native enzyme. The enzyme degraded oligonucleotides and high molecular nucleotides stepwise from the 3'-termini to give 5'-mononucleotides. The enzyme hydrolyzed single-stranded DNA more preferentially than double-stranded DNA. The enzyme also nicked superhelical covalently closed circular phi X174 DNA to yield first open circular DNA and then linear DNA.

Chromatography, Affinity↗

PubMed1972

The erythrasma microorganism in situ: studies using the skin surface biopsy technique.

The skin surface biopsy technique has been used to investigate the erythrasma organism in situ in the stratum corneum in 11 patients. Staining by PAS and Gram stain showed the presence of a large number of organisms arranged haphazardly in some areas and in microcolonies in others. With the scanning electron microscope it was possible to see that smooth filamentous chains of microorganisms had penetrated horn cells and caused disturbance of the surface structure of these cells.Enzyme histochemical tests showed that the erythrasma microorganism possessed a strong reactivity for NAD diaphorase and other mitochondrial enzymes. The reactivity was focal confirming a complex subcellular organization of organelles. It is suggested that the erythrasma microorganism secretes a mucopolysaccharide sheath in some circumstances.

Adult↗

PubMed1992

Modulation of bronchial reactivity by angiotensin-converting enzyme in unanesthetized guinea pigs.

To investigate the role of angiotensin-converting enzyme (ACE) in the modulation of bronchial reactivity, we tested the effects of a specific ACE inhibitor, captopril (CAP), on the bronchial reactivity to substance P (SP) and methacholine (MCH) in unanesthetized guinea pigs. The relative role of ACE on the vascular endothelium and ACE in the airway tissue was examined by administering CAP as an intravenous infusion and by an inhaled aerosol. Bronchial reactivity was evaluated by a provocative dose of SP or MCH at a concentration that would double the baseline value of the specific airway resistance (PC200 or PD200). Neither pretreatment with infused CAP (10 mg/kg) nor inhaled CAP (5 mg) enhanced bronchial reactivity to inhaled SP, whereas the reactivity to infused SP (7.5 x 10(-3) to 20 nM/kg) was enhanced significantly by pretreatment with infused CAP (10 mg/kg) (p less than 0.05). The infusion of CAP (10 mg/kg) also enhanced the bronchial reactivity to both infused MCH (0.05 to 25 micrograms/kg) and inhaled MCH (0.05 to 25 mg/ml) (both p less than 0.05). However, the inhalation of CAP (5 mg) did not affect the bronchial reactivity to inhaled MCH. These observations suggest that ACE located on the vascular endothelium may modulate bronchial reactivity.

Airway Resistance↗

PubMed1976

[Sulfhydryl groups of L-asparaginase A from Pseudomonas fluorescens AG].

It has been demonstrated that the activity of asparaginase A from Ps. fluorescens AG is completely inhibited by 10(-4) M p-chloromercurybenzoate and by 70-85% by Zn2+, Ca2+ and Cu2+ (2.10(-2) M). Iodoacetate, iodoacetamide, N-ethylimide of maleic acid and 5,5'-dithiobis-(2-nitrobenzoic acid) do not decrease the enzyme activity. Dithiothreitol and beta-mercaptoethanol reactivate the enzyme. L-asparagine, the substrate of asparaginase, protects the enzyme in a large degree against the inhibitory action of p-chloromercurybenzoate. p-chloromercurybenzoate induces a sharp increase in the asparaginase inactivation rate at acidic (6.5--5.5) and alkaline (7.5-8.5) values of pH. The enzyme modification by p-chloromercurybenzoate does not change the Km value for L-asparagine, but decreases Vmax. Thus it may be assumed, that asparaginase from Ps. fluorescens AG contains sulfhydryl groups essential for the enzyme activity.

Asparaginase↗

PubMed1989

Detection of membrane-bound alpha-fetoprotein in human hepatoma cell lines by monoclonal antibody 19F12.

Monoclonal antibodies against human alpha-fetoprotein (AFP) were obtained by the hybridoma technique and studied with regard to their reactivities with the human hepatoma cell lines PLC/PRF/5 and KN, and a spontaneously immortalized cell line derived from fetal liver, NuE, all of which synthesize AFP. One of the monoclonal antibodies, 19F12 (IgG2b) became bound to free AFP which was used as the immunogen with an affinity constant of 3.4 X 10(8) M-1. This value was not much higher than those of two other antibodies, 19B1 (IgG1) and 9D12 (IgG2b). However, only antibody 19F12 showed definite reactivity with AFP-producing cells in analysis using flow cytometry. Immunofluorescence microscopy showed that antibody 19F12 detected AFP over the surface of NuE and PLC/PRF/5 cells with a uniform distribution, whereas definite reactivities of antibodies 19B1 and 9D12 to these cells were not detected. These antibodies did not show the specific binding to a non-AFP-producing human lung cancer cell line, PC-9, or to human peripheral blood lymphocytes. The binding ability of 19F12 to hepatoma cells was shown in both viable and fixed cells. Addition of free AFP inhibited the binding of antibody 19F12 to PLC/PRF/5 cells in a concentration-dependent manner. The specific reactivity of 19F12 to human AFP was also confirmed by immunostaining of a tissue section of human cancer proved to be AFP positive with AFP-specific antisera. In two-dimensional polyacrylamide gel electrophoresis of the antigen (from membrane fraction of PLC/PRF/5 cells)-antibody (19F12) complex, spots derived from the antibody and a spot (pI 4.7, Mr 65,000) corresponding in pI and molecular weight to AFP were detected. Western blot analysis showed that material in the membrane fraction of PLC/PRF/5 cells recognized by antibody 19F12 has the same molecular weight as human AFP derived from placenta. In a study of reactivities to PLC/PRF/5 cells treated with various enzymes, the reactivity of this antibody decreased when cells were treated with protease and trypsin and increased when lipase was used. The binding of 19F12 to AFP was not inhibited by concanavalin A. The antibody 19F12 appeared to recognize an epitope that is considered to be part of the peptide area of AFP. These results indicate that the reactivity, the amount of bound antibodies, and the distribution of monoclonal antibodies on antigen-producing cells vary, respectively, even though these antibodies were produced using the same antigen as an immunogen.(ABSTRACT TRUNCATED AT 400 WORDS)

Antibodies, Monoclonal↗

PubMed1988

Purification and characterization of a ribonuclease from human liver.

The major ribonuclease of human liver has been isolated in a four-step procedure. The protein appears homogeneous by several criteria. The amino acid composition and the amino-terminal sequence of the enzyme indicate that the protein is related to human pancreatic ribonuclease and to angiogenin, and that it may be identical with an eosinophil-derived neurotoxin and to a ribonuclease that has been isolated from urine. The catalytic activity of the liver ribonuclease and its sensitivity to iodoacetic acid inactivation also relate the enzyme to the pancreatic RNases, but the liver protein is clearly differentiated by immunological measurements. Antibodies to the liver ribonuclease inhibit its activity, but not that of the human pancreatic enzyme; cross-reactivity in a radioimmunological assay is small but measurable. Immunochemical measurements have been used to examine the distribution of the liver-type protein in other tissues. Inhibition of enzyme activity by anti-liver ribonuclease shows that a cross-reactive enzyme is predominant in extracts of spleen and is a significant component in kidney preparations, while the liver-type protein is almost absent in brain or pancreas homogenates. Cross-reactive ribonuclease is present in serum, but levels are not correlated with any of the disease states examined.

Amino Acid Sequence↗

PubMed2005

The intrinsic axial ligand effect on propene oxidation by horseradish peroxidase versus cytochrome P450 enzymes.

The axial ligand effect on reactivity of heme enzymes is explored by means of density functional theoretical calculations of the oxidation reactions of propene by a model compound I species of horseradish peroxidase (HRP). The results are assessed vis-a-vis those of cytochrome P450 compound I. It is shown that the two enzymatic species perform C=C epoxidation and C-H hydroxylation in a multistate reactivity scenario with Fe(III) and Fe(IV) electromeric situations and two different spin states, doublet and quartet. However, while the HRP species preferentially keeps the iron in a low oxidation state (Fe(III)), the cytochrome P450 species prefers the higher oxidation state (Fe(IV)). It is found that HRP compound I has somewhat lower barriers than those obtained by the cytochrome P450 species. Furthermore, in agreement with experimental observations and studies on model systems, HRP prefers C=C epoxidation, whereas cytochrome P450 prefers C-H hydroxylation. Thus, had the compound I species of HRP been by itself, it would have been an epoxidizing agent, and at least as reactive as cytochrome P450. In the enzyme, HRP is much less reactive than cytochrome P450, presumably because HRP reactivity is limited by the access of the substrate to compound I.

Alkenes↗

PubMedDate not supplied

Human placental 5'-nucleotidase: purification and properties.

Subcellular fractionation of human term placenta showed that the highest relative specific activity of 5'-nucleotidase and alkaline phosphatase resided in the microsomal fraction; of the total 5'-nucleotidase activity present, 7 per cent was in the cytosol. 5'-Nucleotidase was reproducibly purified over 500-fold in 17 per cent yield from the insoluble component of homogenates of term placenta to give a single major glycoprotein with two minor inactive protein contaminants. Purified placental 5'-nucleotidase was free from non-specific or alkaline phosphatase, hydrolysed 12 to 22 mumol AMP/min/mg of protein at 30 degrees C, and was activated up to fivefold by Triton X-100. AMP, Km 5 to 7 microM, was the preferred substrate. The Arrhenius plot was biphasic, with activation energies of 21.7 and 49.7 kJ/mol above and below 36 degrees C, the region of the transition temperature. Nucleoside di- and triphosphates inhibited competitively; the most potent inhibitors were ADP and adenosine 5'-methylenediphosphonate, Ki slope 90 nm and 6 nm, respectively. Lectins inhibited the enzyme; concanavalin A caused time-dependent inactivation reversible by alpha-methyl-D-mannoside. EDTA inactivated the enzyme; partial reactivation was achieved with divalent cations. The pH optimum was 7.2 to 7.3; Mg2+ produced a second alkaline pH optimum. The properties of placental 5'-nucleotidase are those of an intrinsic membrane protein and, in general, resemble properties of the several 'ecto'-5'-nucleotidases which have been purified from other tissues, although certain differences in kinetic properties of the placental enzyme are apparent.

5'-Nucleotidase↗

PubMed1990

Selective neuronal glycoconjugate expression in sensory and autonomic ganglia: relation of lectin reactivity to peptide and enzyme markers.

Several plant lectins were used to characterize the cell-surface carbohydrates expressed on sensory ganglion cells and their central terminals in the spinal cord dorsal horn. In the rat, galactose-terminal glycoconjugates on a large subpopulation of small neurons whose central axons project to the substantia gelatinosa were demonstrated with the alpha-D-galactose-specific Griffonia Simplicifolia I-B4 (GSA) lectin. This neuron subset was labelled by alternative D-galactose-, N-Acetylgalactosamine-, and beta Gal(1,3)NAcGal-binding lectins. Similar GSA lectin reactivity was also illustrated in selected peripheral autonomic, gustatory and visceral sensory and enteric neurons, and the accessory olfactory bulb. The sensory neuron-specific isoenzyme, fluoride-resistant acid phosphatase (FRAP) co-localized with the GSA lectin, as did the monoclonal antibody (MAb) 2C5, which is directed against a lactoseries carbohydrate constituting a backbone structure of ABH human blood group antigens. In contrast, calcitonin gene-related peptide-immunoreactivity (CGRP-IR), used as a representative marker of peptidergic neurons, exhibited limited co-localization with GSA. A polyclonal anti-rat red blood cell (RBC) antibody co-localized with GSA, suggesting that lectin-reactive carbohydrates on rat sensory neurons are related to rat RBC antigens. In the human spinal cord, the L-fucose-binding Ulex europaeus-I (UEA) lectin also labelled the substantia gelatinosa; in rabbit, a small sensory ganglion cell subset and the spinal cord substantial gelatinosa was co-labelled by both the GSA and UEA lectins. These studies illustrate significant lectin-reactive cell surface carbohydrate expression by non-peptidergic, FRAP(+) sensory ganglion cells in the rat, and provide a means for visualizing the extensive, non-peptidergic, small sensory ganglion cell subpopulations, probably including a substantial proportion of nociceptive and unmyelinated peripheral axons.

Acid Phosphatase↗

PubMed1981

Dissociation and reassociation of prolyl 4-hydroxylase subunits after cross-linking of monomers.

1. Incubation of prolyl 4-hydroxylase (prolyl-glycyl-peptide, 2-oxoglutarate : oxygen oxidoreductase (4-hydroxylating), EC 1.14.11.2) with H2O2 leads to a decrease of 50% in the specific activity of enzyme tetramers, followed by dissociation into inactive dimers in which the monomers are covalently cross-linked by S-S bridge formation. 2. Incubation of the enzyme with K3Fe(CN)6 leads to a comparable decrease in activity of enzyme tetramers. Addition of urea leads to dissociation into inactive dimers with similarly cross-linked monomers. 3. Removal of the dissociating agent leads to reassociation of cross-linked dimers to tetramers and to about 50% reactivation. The enzyme is further reactivated by preincubation with dithiothreitol. 4. Dissociation of the enzyme with dithiothreitol, urea or LiCl, or at low pH (4.15) produces inactive monomers, which could not be reassociated.

Animals↗

PubMed1989

Diagnostic specificity, sensitivity and cross-reactivity of an enzyme-linked immunosorbent assay for the detection of antibody against Leptospira interrogans serovars pomona, sejroe and hardjo in cattle.

Outer sheath antigen was prepared from Leptospira interrogans serovars pomona, sejroe and hardjo by treating the organisms with 1.0M NaC1 followed by 0.04% sodium dodecyl sulfate (SDS). Sodium dodecyl sulfate was removed from the SDS-protein complexes by the extraction of dodecyl sulfate anions as ion pairs with triethylammonium cations into an organic solvent. The outer sheath antigen was recovered from the organic solvent as a precipitate and used as the source of leptospiral enzyme-linked immunosorbent assay (ELISA) antigen. Utilizing this antigen, ELISA was adapted to detect bovine serum antibody to L. interrogans serovars pomona, sejroe and hardjo. The specificity of this assay in 344 bovine sera, which were negative in the microscopic agglutination test (MAT) for seven serovars, was 99.4%. In sera from 37 and 87 cattle which revealed MAT titers greater than or equal to 1:50 for L. interrogans serovars pomona and sejroe, the relative sensitivity of the test was 100%. The ELISA also showed a considerable degree of low level cross-reactivity with other serovars. Sixty-six (75.9%) out of 87 bovine sera which were MAT-positive (MAT titer of greater than or equal to 1:50) with serovars sejroe and hardjo only were ELISA positive with heterologous pomona antigen; 16 (43.2%) and six 16.2%) out of 37 bovine sera which were MAT positive MAT titer of greater than or equal to 1:50) with serovar pomona only were ELISA positive with heterologous sejroe and hardjo ELISA antigen respectively.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

PubMed1987

Comparison of indirect immunofluorescence and Western blot for detection of anti-human immunodeficiency virus antibodies.

There was 100% agreement between the results of indirect immunofluorescence (IF) and Western blot testing when these methods were used to detect antibodies to the human immunodeficiency virus in sera from 25 patients with acquired immune deficiency syndrome (AIDS), 20 patients with AIDS-related complex, 186 subjects at high risk for AIDS, and 40 healthy heterosexuals. However, there was only an 88.7% correlation between IF and Western blot results for 728 sera from blood and plasma donor centers that were selected on the basis of screening enzyme immunoassay reactivity. IF tests yielded nine false-negatives and were equivocal, yielding a nonspecific pattern of reactivity for both infected and uninfected cells for 73 of these specimens. The IF and Western blot methods were equal in performance for the detection of anti-human immunodeficiency virus antibodies in the high-risk and unselected low-risk groups, proving to be a practical approach for testing specimens from these subjects. However, the Western blot was the most acceptable method for the validation of specimens from groups at low risk for AIDS that were selected based on enzyme immunoassay reactivity.

AIDS-Related Complex↗