Disease relevance of CCRIS 4590

• The kinetics of 9-aminoacridine (9-AA) block of single Na channels in neuroblastoma N1E-115 cells were studied using the gigohm seal, patch clamp technique, under the condition in which the Na current inactivation had been eliminated by treatment with N-bromoacetamide (NBA) [1].
• The use of substances (N-bromoacetamide, trypsin, chloramine-T, and papain) that remove the inactivation of Na+ and K+ currents in other cells are not effective in removing the inactivation of K+ currents present in this lymphoma cell line [2].

High impact information on CCRIS 4590

• Calcium-activated potassium channels from cultured rat skeletal muscle were treated with the protein-modifying reagent N-bromoacetamide (NBA) (0.3-1 mM) and studied in excised patches using patch-clamp techniques [3].
• We have studied the effect of N-bromoacetamide (NBA) on the behavior of single sodium channel currents in excised patches of rat myotube membrane at 10 degree C. Inward sodium currents were activated by voltage steps from holding potentials of about -100 mV to test potentials of -40 mV [4].
• The alkylation reaction was tested using N-(beta-chitotriose) bromoacetamide and an unprotected synthetic hexapeptide containing a single cysteine residue [5].
• Quantification of exponential Na+ current activation in N-bromoacetamide-treated cardiac myocytes of guinea-pig [6].
• N-bromoacetamide (NBA) and N-bromosuccinimide (NBS), reagents which remove inactivation gating in physiological preparations, transiently stimulate the sodium permeability of inside-out facing channels to high levels [7].

Biological context of CCRIS 4590

• Pepsin was spin-labelled with N-(1-oxyl-2,2,6,6-tetramethyl-4-piperidyl) bromoacetamide, possibly at the active site, at a beta-catboxyl group of a reactive aspartic acid [8].

Anatomical context of CCRIS 4590

• N-bromoacetamide removes a calcium-dependent component of channel opening from calcium-activated potassium channels in rat skeletal muscle [3].
• The kinetics of strychnine block of single Na channels in bovine chromaffin cells were studied using the gigohm seal, patch-clamp technique, under the condition in which the Na current inactivation had been eliminated by treatment with N-bromoacetamide (NBA) [9].
• 3. The ultrastructure of hepatopancreas cells are markedly influenced by bromoacetamide, including swelling of mitochondria and splitting of cristae [10].

Associations of CCRIS 4590 with other chemical compounds

• Similarly, alkylation of papain with methyl bromoacetate exhibits no kinetic isotope effect, whereas for the analogous alkylation with bromoacetamide an inverse isotope effect is observed [11].
• The binding and alkylation rate constants for the reaction of four bromoacetamido pyrimidine nucleosides and bromoacetamide with bovine pancreatic ribonuclease A (RNase A) have been determined as a function of temperature [12].

Gene context of CCRIS 4590

• Introduction of the electrophilic isothiocyanate and bromoacetamide groups on the para position of Phe3 and Phe5 was accomplished by incorporating Fmoc-Phe(p-NHAlloc) into the peptide followed by selective deprotection and modification [13].
• Bromoacetamide derivatives having n-alkyl substituents (BrCH2CONH(CH2)nH, 1-n) and carboxyalkyl substituents (BrCH2CONH(CH2)nCOOH, 2-n) react with His-15 in lysozyme exclusively at N epsilon 2 at pH 5.5 and 40 degree C. Kinetic studies suggest that lysozyme has a small hydrophobic pocket that binds these reagents in the vicinity of His-15 [14].
• Enthalpic and entropic determinants for the specificity of alkylation of the histidine-12 residue of ribonuclease A by four bromoacetamido nucleoside affinity labels and bromoacetamide [12].

Analytical, diagnostic and therapeutic context of CCRIS 4590

• After treatment with either a proteolytic enzyme such as papain or the amino acid reagent N-bromoacetamide, the K current no longer inactivated rapidly, but decayed very slowly with a time constant of 500 to 750 ms [15].

References