Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0040822 (tremor)
 18,428 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We reported a 65-year-old man whose sister was suffering from HTLV-I-associated myelopathy (HAM) and who presented slowly progressive spastic paraparesis, sensory disturbance in the feet, tremors and cerebellar ataxia. He was also positive for serum anti-HTLV-I antibody. He first showed a head tremor at the age of 3 years. He developed a spastic and ataxic gait when aged 15 years, and it became difficult for him to walk at the age of 50 years. Examination at 65 years showed a spastic and ataxic gait and scanning speech. Hyper-reflexia and Bahinski's signs were observed. Sensation in the feet was decreased. The anti-HTLV-I antibody titer in the serum was 1:512 by the PA method, and Western blot analysis revealed bands of P19, P24, P28 and P32. Examination of the cerebrospinal fluid (CSF), including oligoclonal bands, gave normal results. The CSF was negative for anti-HTLV-I antibody. CT and MRI of the head showed cerebellar atrophy. His sister was 60 years old. She had developed a spastic gait at the age of 15 years. Sensory defects and bladder dysfunction developed when aged 35 years. Hyper-reflexia, Babinski's sign and foot clonus were observed. Sensation in the feet was decreased. The urinary residual volume was increased. Ataxia was not observed. The anti-HTLV-I antibody titer in the serum was 1:8,192 by the PA method, and Western blot analysis revealed bands of p24, p28 and p32. Examination of the CSF, including oligoclonal bands, gave only normal results.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Spastic paraparesis and sensory disturbance improved by prednisolone therapy]. 139 32

The immune complex transfer enzyme immunoassays for antibody IgGs to p17, p24, and reverse transcriptase (RT) of HIV-1 were tested under various conditions. Antibody IgGs to HIV-1 were reacted for up to 20 hr with 2,4-dinitrophenyl-bovine serum albumin-recombinant HIV-1 protein conjugates and recombinant HIV-1 protein-beta-D-galactosidase conjugates, and the immune complexes formed, comprising the three components, were trapped onto polystyrene beads coated with (anti-2,4-dinitrophenyl group) IgG by incubation at 4-30 degrees C for up to 2 hr with shaking and were transferred onto polystyrene beads coated with (antihuman IgG gamma-chain) IgG in the presence of excess of epsilon N-2,4-dinitrophenyl-L-lysine by incubation at 4-30 degrees C for up to 2 hr with shaking. When serum randomly collected from an HIV-1 seropositive subject and serum included in an Western blot kit were tested, the formation of the immune complex was almost completed within 1 hr for antibody IgG to p17, within 1-2 hr for antibody IgG to p24 and within 4 hr for antibody IgG to RT. Even for antibody IgG to p17, however, the immune complex continued to be formed for at least 2 hr, when serum samples at early stages of HIV-1 infection were tested. Trapping and transferring of the immune complexes were faster at higher temperatures and were almost completed within 0.5-1.5 hr, although the amount of the immune complexes trapped and transferred at 25 and/or 30 degrees C increased for 0.5-1 hr, but subsequently tended to decline. When the formation, trapping, and transferring of the immune complexes were performed for 0.5, 1, and 1 hr, respectively, with shaking followed by 1 hr assay of bound beta-D-galactosidase activity, the sensitivities for antibody IgGs to p17, p24, and RT using 10 microliters of serum samples were similar to or significantly higher than those of the corresponding previous immune complex transfer enzyme immunoassays using 10 microliters of serum samples, in which the formation, trapping, and transferring of the immune complexes were performed for 3, 16, and 3 hr, respectively, without shaking, followed by 2.5 hr assay of bound beta-D-galactosidase activity, and the sensitivities for antibody IgGs to p17, p24, and RT using 100 microliters of serum samples were 21-22-fold, 5.5-6.3-fold, and 5.3-6.0-fold, respectively, higher. When each period of time for the formation, trapping, and transferring of the immune complexes was prolonged to up to 4 hr, the sensitivities for antibody IgGs to p17, p24, and RT using 100 microliters of serum samples were improved 88-93-fold, 15-17 fold and 20-24-fold, respectively, as compared with those of the previous ones.
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PMID:Optimal conditions of immune complex transfer enzyme immunoassays for antibody IgGs to HIV-1 using recombinant p17, p24, and reverse transcriptase as antigens. 952 94

In the immune complex transfer enzyme immunoassay for HIV-1 p24 antigen, different preparations of anti-p24 Fab'-beta-D-galactosidase conjugate, various periods of time for immunoreactions involved, and shaking for incubations with polystyrene beads were tested. On the basis of the results of these experiments, p24 antigen was measured as follows. The antigen was reacted simultaneously with 2,4-dinitrophenyl-biotinyl-bovine serum albumin-affinity-purified rabbit anti-p24 Fab' conjugate and highly polymerized monoclonal mouse anti-p24 Fab'-beta-D-galactosidase conjugate at 37 degrees C for 2 hr. The immune complex formed comprising the three components was trapped onto colored polystyrene beads coated with affinity-purified (anti-2,4-dinitrophenyl group) IgG for 1.5 hr and was transferred to white polystyrene beads coated with streptavidin in the presence of epsilon N-2,4-dinitrophenyl-L-lysine for 1.5 hr. The incubations with polystyrene beads were performed at room temperature with shaking. beta-D-Galactosidase activity bound to the white polystyrene beads was assayed by fluorometry at 30 degrees C for 2 hr. The detection limit of p24 antigen (0.1 amol/tube and 10 amol (0.24 pg)/ml of serum) was equal to that obtained when the formation, trapping, and transferring of the immune complex were performed for 4, 16, and 3 hr, respectively, by incubation without shaking. Namely, the period of time required for the immune complex transfer enzyme immunoassay of p24 antigen was markedly shortened (25.5-7 hr) without loss of the sensitivity. By the improved immune complex transfer enzyme immunoassay, p24 antigen was detected 12-20 days earlier than the detection of antibodies to HIV-1, i.e., seroconversion by the conventional ELISA.
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PMID:Optimal conditions of immune complex transfer enzyme immunoassay for p24 antigen of HIV-1. 952 96

The immune complex transfer enzyme immunoassay for HIV-1 p24 antigen was performed in three different ways (in the present immunoassays I, II, and III) within much shorter periods of time than previously reported. In the present (simultaneous) immunoassay I, p24 antigen was incubated simultaneously with 2,4-dinitrophenyl-biotinyl-bovine serum albumin-affinity-purified rabbit anti-p24 Fab' conjugate and monoclonal mouse anti-p24 Fab'-beta-D-galactosidase conjugate in a total volume of 19 microL for 15 min to form the immune complex comprising the three components. The reaction mixture was incubated with a polystyrene bead of 6.35 mm in diameter coated with affinity-purified (anti-2,4-dinitrophenyl group) IgG for 5 min to trap the immune complex. After washing, the polystyrene bead was incubated with 35 microL of epsilonN-2,4-dinitrophenyl-L-lysine for 15 min to elute the immune complex (the first eluate) and, after removing the first eluate, with an additional 35 microL of epsilonN-2,4-dinitrophenyl-L-lysine for 1 min (the second eluate). The first and second eluates were incubated with a polystyrene test tube (12 x 75 mm) coated with streptavidin for 15 min. In the present (sequential) immunoassay II, a polystyrene bead of 6.35 mm in diameter successively coated with affinity-purified (anti-2,4-dinitrophenyl group) IgG and 2,4-dinitrophenyl-biotinyl-bovine serum albumin-affinity-purified rabbit anti-p24 Fab' conjugate was incubated with p24 antigen in a total volume of 20 microL for 5 min and subsequently with monoclonal mouse anti-p24 Fab'-beta-D-galactosidase conjugate in a volume of 5 microL for 20 min. The immune complex formed on the polystyrene bead was transferred to a polystyrene test tube coated with streptavidin as described above. In the present (sequential) immunoassay III, p24 antigen was incubated with monoclonal mouse anti-p24 Fab'-beta-D-galactosidase conjugate in a total volume of 19 microL for 10 min and with a polystyrene bead of 6.35 mm in diameter coated successively with affinity-purified (anti-2,4-dinitrophenyl group) IgG and 2,4-dinitrophenyl-biotinyl-bovine serum albumin-affinity-purified rabbit anti-p24 Fab' conjugate for 20 min. The immune complex formed on the polystyrene bead was transferred as described above. The incubations were performed at room temperature either by shaking the polystyrene beads (one/assay) and the reaction mixtures in styrol test tubes (13.3 x 54 mm and 2.1 g) so as to randomly rotate the polystyrene beads or by rotating the polystyrene test tubes (12 x 75 mm) containing the reaction mixtures, so that small drops (19 to 70 microL) of the reaction mixtures evenly contacted all parts of the solid phase surfaces during the incubations (although they contacted only small parts of the solid phase surfaces at a time) to continuously mix thin aqueous layers covering the solid phase surfaces with the rest of the reaction mixtures. (Therefore, these immunoassays are called thin aqueous layer immunoassays.) The detection limits of p24 antigen by 1 hr assay of bound beta-D-galactosidase activity in the present immunoassays I, II, and III were 0.1, 0.2 and 0.1 amol/assay, respectively, and were slightly higher than or equal to that by the previously reported immune complex transfer enzyme immunoassay, in which the immune complex was formed for 4 hr, was trapped for 16 hr, and was transferred for 3 hr followed by 1-hr assay of bound beta-D-galactosidase activity. By 20-hr assay of bound beta-D-galactosidase activity, the detection limit of p24 antigen was further lowered to 10 zmol/assay in the present (simultaneous) immunoassay I and to 3 zmol/assay in the present (sequential) immunoassay III. However, the nonspecific reaction(s) with serum samples from HIV-1 seronegative subjects hampered the improvement of the detection limit by 20-hr assay of bound beta-D-galactosidase activity.
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PMID:Rapid and ultrasensitive enzyme immunoassay (thin aqueous layer immune complex transfer enzyme immunoassay) for HIV-1 p24 antigen. 967 Nov 71

The clinical sensitivity of the current anti-HIV assays is based for an important part on their reactivity with seroconversion panels. The most sensitive assay closes the seroconversion window as much as possible, thereby reducing the risk of transmitting false negative donations obtained from individuals infected recently. Because of the absence of anti-HIV antibodies during the early phase of infection, the seroconversion window can be narrowed partially by detection of HIV p24 Ag. To achieve this, the highest affinity anti-p24 binding antibodies were selected with BlAcore and applied in a direct assay format. To achieve optimal conditions for the anti-HIV part of the assay the HIV specific antigens viral HIV-1 gp160, HIV-2 gp36 and HIV-1 group O gp41 peptides were used. These antigens and antibodies were applied for microELISA coating as well as in the conjugate pearl, which is present in the well of the microELISA plate. The (analytical) anti-HIV-1/-2 and anti-HIV-1 group O sensitivity of this new assay, Vironostika HIV Uni-Form II Ag/Ab, is at least at the level of the current Vironostika HIV Uni-Form II plus O. When compared to the Vironostika HIV Uni-Form II plus O, the seroconversion window is narrowed by 1-2 weeks due to the incorporation of HIV p24 Ag detection. The level of reactivity of the anti-HIV and HIV Ag detection part can be improved by about a factor 2 by applying continuous shaking during sample incubation. Initial studies suggested that the specificity of the assay is identical to that of the Vironostika HIV Uni-Form II plus O, namely > 99.9%. Monitoring of proper execution of the assay handling steps was facilitated by implementing a purple dye in the conjugate pearl. Colourless specimen diluent changes into a green fluid upon dissolving of the conjugate pearl and turns subsequently into blue/purple upon sample addition. These visual changes can also be determined by spectrophotometric measurement at 620 nm.
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PMID:Strongly enhanced sensitivity of a direct anti-HIV-1/-2 assay in seroconversion by incorporation of HIV p24 ag detection: a new generation vironostika HIV Uni-Form II. 992 40

A gene for autosomal dominant familial essential tremor maps to a 9.1 cM interval flanked by loci D2S224 and D2S405 (ETM2) on human chromosome 2p24.3-p24.2. The recombinatorial boundaries of the interval were refined on a radiation hybrid map to a 123 cR minimal critical region (MCR) between D2S224 and D2S2221. High-throughput non-isotopic screening of bacterial artificial chromosomes (BACs) was used to assemble a physical map of the region. A scaffold BAC map of 31 overlapping clones was ordered by their sequence tagged site (STS) content using PCR and Southern blotting. A complementary 3.9 Mb integrated physical map of the human ETM2 region was constructed by identifying GenBank contigs that contained seven BAC DNA sequences and common STSs. Thirty-three transcripts including five known genes (MATN3, LAPTM4A, SDC1, PUM2, and APOB) were identified in the MCR and ordered on an integrated contig by PCR and virtual mapping. This physical map will provide a template for genomic sequencing and the identification of a gene for essential tremor.
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PMID:Integrated physical map of the human essential tremor gene region (ETM2) on chromosome 2p24.3-p24.2. 1510 95