Disease relevance of Trizma

• Substituting TRIS buffer for bicarbonate in the infusion also eliminated acidosis, but neither concentrations of 1 M or 5 M buffers prevented the stomachs from ulceration (6 out of 6 with 1 M buffer and 5 of 6 with 5 M buffer) [1].
• Because a majority of duodenal-ulcer patients responded locally to intradermal secretin, skin samples from 7 patients with duodenal ulceration and 6 patients with goitre or cholelithiasis were incubated with "tris" buffer alone and with tris buffer containing 20 C.U./ml synthetic secretin or 100 microng/ml compound 48/80 [2].
• Coronary arterial spasm and Prinzmetal's variant form of angina induced by hyperventilation and Tris-buffer infusion [3].
• The enzyme from Escherichia coli has been crystallized by the vapor diffusion method from Tris buffer (pH 8.5) using polyethylene glycol 4000 as a precipitant [4].
• The metabolism of platelet activating factor (PAF) by lungs of near-term fetal and 5- to 9-day-old lambs was studied during normoxia and hypoxia at 37 degrees C in 30 mM Tris buffer [5].

High impact information on Trizma

• The crystal and molecular structure of the widely used buffer tris(hydroxymethyl)aminomethane (tris) has been determined from single-crystal diffractometer data to a standard agreement factor (R value) of 0.026 and bond length standard deviations of 0.002 angstrom [6].
• This potentiation did not occur for MRA treated with boiled microsomes and NADPH, active microsomes in the absence of NADPH, or Tris buffer plus NADPH [7].
• After solubilization in 8.5 M urea, in vitro filament reconstitution is induced when urea is removed by dialysis against 2-50 mM Tris buffer at pH 7 [8].
• Vigorous hyperventilation was induced for five minutes immediately after a five-minute infusion of 100 ml of Tris-buffer (pH 10) in nine patients with Prinzmetal's variant angina [3].
• Urea Tris buffer-dissolved fibrin monomers were injected into the pulmonary artery in the presence of circulating excess fibrinogen [9].

Chemical compound and disease context of Trizma

• Two previously unidentified ubiquitinated proteins with molecular masses of 10 and 17 kDa were found in 8 M urea-soluble extracts, obtained from Tris-buffer-insoluble materials, of acute myeloid leukemia OCI/AML 1a cells and the cells from the leukemia patients [10].
• Five major outer membrane proteins (D1, D2, E, G, and H1) of Pseudomonas aeruginosa, but not proteins F (porin), I (lipoprotein), and H2, were detected in high-molecular-weight protein-lipopolysaccharide complex(es) solubilized from sucrose-stabilized cells on exposure to ethylenediaminetetraacetate and tris(hydroxymethyl)aminomethane [11].
• Epithelioma papillosum carpio cells were grown in normal atmosphere with tris(hydroxymethyl)aminomethane- or HEPES (N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid)-buffered media [12].
• Twenty-six attacks with S-T segment depression included 3 induced by methacholine, 13 by arm exercise, 3 by hyperventilation with or without Tris-buffer infusion and 7 by ergonovine maleate [13].
• The S15 myeloma protein in 0.05 M Tris buffer at pH 7.4 precipitated dextran sulfate, heparin, chondroitin sulfate A, B and C, hyaluronic acid, H. influenzae type b polysaccharide, calf thymus DNA, Klebsiella polysaccharide K63 and poly-L glutamic acid [14].

Biological context of Trizma

• From the measurements at different concentrations of TRIS buffer acting as proton exchange catalyst, base pair lifetimes were evaluated [15].
• From this we conclude that poly (rG-m5dC).poly (rG-m5dC) is in a regular A conformation in Tris buffer at low Na+ levels, shifting to an alternating A conformation with a dinucleotide repeat at intermediate salt concentrations [16].
• These observations were made when intact cells were incubated either in a buffer which supported glycolysis or in a simple isotonic Tris buffer without glucose [17].
• Quenching of bithiazole fluorescence by DNA was used to determine apparent equilibrium constants for the complex which, in 2.5 mM tris(hydroxymethyl)aminomethane buffer, pH 8.4, are 1.2 X 10(5) M-1 for bleomycin and 1.4 X 10(5) M-1 for tripeptide S, a partial acid hydrolysis product of the antibiotic [18].
• The IC50 was 1-2 mM under a variety of conditions (i.e., whole tissue or synaptic membranes, frozen/thawed or fresh, D-[3H]aspartate (10-1000 nM) or L-[3H]glutamate (100 nM), phosphate or Tris buffer, NaCl or Na acetate, presence or absence of Ca2+ and Mg2+) [19].

Anatomical context of Trizma

• Soluble cell membrane extracts were prepared in a Tris buffer with protease inhibitors, immunoprecipitated, electrophoresed, and immunoblotted with an antiserum to EGF receptors [20].
• Abnormal amounts os Hb A and Hb AI resisted removal from diabetic red-cell membranes by low ionic buffers but yielded to hypotonic Tris buffer [21].
• Tris(hydroxymethyl)aminomethane inhibits the synthesis and processing of proinsulin in isolated rat pancreatic islets without affecting release of insulin stores [22].
• Incubation of adipocytes with insulin in Tris buffer (100 ng/ml) resulted in a 40-60% decrease in cell surface insulin binding capacity [23].
• The animals received either PGI2 in Tris buffer solution (20 to 40 ng/kg per min, n = 14) or Tris buffer alone (control, n = 14) beginning 10 minutes after anterior descending coronary artery occlusion [24].

Associations of Trizma with other chemical compounds

• Ghosts prepared in 0.1 mM EDTA and 17 mM Tris buffer (pH 7.5) have about 230 molecules of phosphoglycerate kinase/ghost [25].
• The corneal explants with macular corneal dystrophy also synthesized prominent fractions which eluted from DEAE-Sephacel columns in 0.05 M tris(hydroxymethyl)aminomethane buffer (pH 7.2) with 0.15 M and/or 0.25 M lithium chloride after pronase digestion [26].
• The mild conditions used for elution from the column, 0.5% deoxycholate in 10 mM Tris buffer, pH 8, with 0.14 M NaCl, result in recovery of 70 to 100% of the allogeneic serological activity [27].
• This reaction showed a pH optimum at 6.5 to 7.0 in 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid buffer and was inhibited by phosphate buffer and Tris buffer [28].
• The affinity of the hormone-bound estrogen receptor for DNA in Tris buffer at pH 7.4 in 0.2 M KCl is 10-fold greater than at pH 8.0, suggesting that ionic bonding between the receptor and DNA may involve histidine residues of the receptor [29].

Gene context of Trizma

• Sulfonated (Asn55-Ala107) SLPI was refolded in Tris buffer containing reduced and oxidized glutathione [30].
• In the presence of 30 mM Na2SO4/50 mM Tris buffer, SP interacted with two types of binding sites with Kd values of 0.3 and 40 nM [31].
• When native TPP II was dissociated into smaller units through dialysis against a dilute Tris buffer, it could be digested by chymotrypsin into three stable fragments of 70 kDa, 42 kDa and 20 kDa [32].
• The lower ionic strength of the Tris buffer may underlie this effect. hBD-1 kills the M1 strain of GAS only in 10 mm Tris, but is able to kill an M6 (SIC negative) strain in 10 mm phosphate [33].
• After dilution of plasma with low ionic Tris buffer and activation of the protease with barium chloride, a VWF concentrate is digested in the presence of urea [34].

Analytical, diagnostic and therapeutic context of Trizma

• Proteolysis of insulin or (pre)proinsulin with S. aureus protease V8 in Tris buffer at neutral pH yields a characteristic pattern of peptide fragments that is resolved using high-performance liquid chromatography [35].
• Small 1:2 diluted serum or plasma samples are incubated with a tracer dose of tritiated T in pH 7.4 Tris buffer at 37 C then chilled and placed on columns at 4 C. Free and albumin bound T are washed off columns with pH 7.4 Tris buffer and columns are eluted with pH 2 Tris into vials for scintillation counting [36].
• Titration with the base catalyst tris(hydroxymethyl)aminomethane allows the determination of kop, the rate constant for the localized opening of individual base pairs, prior to dissociation [37].
• The circular dichroism spectra of fragments 12A and 12B in 0.2-10 mM Tris buffer are characteristic of B-form DNA [38].
• The purity of the 99mTc complexes was determined by paper electrophoresis in 0.1 M tris buffer [39].

References