High impact information on Bicine

• Metal-ion affinity (formation) constants were determined for two "Good's" buffers, N-tris(hydroxymethyl)methyl-2-aminoethanesulfonic acid (TES) and N,N-bis(2-hydroxyethyl)glycine (bicine) [1].
• All three kringle lysine-binding sites contain a bound bicine molecule of crystallization while the former of kringle 2 and kringle 3 are cofacial [2].
• Rat liver arginase, a manganese-metalloenzyme, has been crystallized from polyethylene glycol 8000 in N,N-bis(2-hydroxyethyl)glycine (Bicine) buffer at pH 8 [3].
• The best buffer of the four examined in this study was bicine; energetics, glycolytic flux, and patterns of adenylate regeneration upon reperfusion were markedly superior to modified UW solution [4].
• Tests of the cell using xanthine oxidase, in 50 mM Bicine buffer, pH 7.7, yielded midpoint potentials of -345 and -371 mV for the Mo(VI)/Mo(V) and Mo(V)/Mo(IV) couples compared with values of -373 and -377 mV obtained by electron paramagnetic resonance analysis of frozen potentiometric samples [5].

Biological context of Bicine

• The metal chelates formed undergo loss of an internal ligand (alcohol) proton (bicine) and undergo hydrolysis (bicine and TES) and dimerization reactions (TES) [1].
• The reductive methylation procedure worked well at pH 8.0-8.5 in either pyrophosphate buffer or Bicine buffer using formaldehyde with [3H]-sodium borohydride as the reducing agent [6].
• A two-stage Bicine-doubled sodium dodecyl sulfate-polyacrylamide gel electrophoresis protocol was designed to separate membrane proteins and circumvent problems associated with membrane protein analysis using traditional gel-based proteomics approaches [7].
• Michaelis-Menten kinetics are observed in studies of highly purified bovine adrenal glucose-6-phosphate dehydrogenase at pH8.0 in 0.1 M bicine [8].

Anatomical context of Bicine

• A strong iron-chelating agent, iminodiacetic acid (IDA), and a weak one, dihydroxyethylglycine (DHEG), decreased iron permeation into preconfluent fibroblasts [9].
• Data are presented and reviewed which indicate that many of the most commonly used artificial buffers (e.g., Tris, HEPES, MOPS, Bicine, PIPES, imidazole) can exert adverse effects on contractility and reactivity of certain arterial and venous smooth muscles [10].

Associations of Bicine with other chemical compounds

• Standard electromotive force of the H2-AgCl;Ag cell in 30, 40, and 50 mass% dimethyl sulfoxide/water from -20 to 25 degrees C: pK2 and pH values for a standard "Bicine" buffer solution at subzero temperatures [11].
• They require however special home-made gels and cannot be applied to several electrophoretic systems (e.g. systems using tricine or bicine as the trailing ion, or isoelectric focusing in immobilized pH gradients) [12].
• Histochemical demonstration of guanase in human liver with guanine in bicine buffer as substrate [13].

Gene context of Bicine

• Bicine and TES buffer not only hydrogen ions but also metal ions [1].
• Imidazoles, Ches and phosphate are thought to participate in a metal center-to-buffer proton transfer pathway, whereas Bicine, Taps, Mops and Mes appear to lack this capacity, so that the rate-limiting proton transfer occurs in a metal center-to-bulk water pathway for these variants [14].

Analytical, diagnostic and therapeutic context of Bicine

• A novel, Bicine-based SDS-PAGE buffer system was developed for the analysis of membrane proteins [15].

References