18103
1-Bromopinacolone
purum, ≥97.0% (GC)
Synonym(s):
1-Bromo-3,3-dimethyl-2-butanone, Bromomethyl tert-butyl ketone
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About This Item
Linear Formula:
(CH3)3CCOCH2Br
CAS Number:
Molecular Weight:
179.05
EC Number:
226-794-0
UNSPSC Code:
12352100
PubChem Substance ID:
Beilstein/REAXYS Number:
506485
MDL number:
grade
purum
assay
≥97.0% (GC)
refractive index
n20/D 1.466
bp
188-194 °C (lit.)
mp
−10 °C (lit.)
density
1.331 g/mL at 25 °C (lit.)
storage temp.
−20°C
SMILES string
CC(C)(C)C(=O)CBr
InChI
1S/C6H11BrO/c1-6(2,3)5(8)4-7/h4H2,1-3H3
InChI key
SAIRZMWXVJEBMO-UHFFFAOYSA-N
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signalword
Warning
hcodes
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
10 - Combustible liquids
wgk
WGK 3
flash_point_f
167.0 °F - closed cup
flash_point_c
75 °C - closed cup
ppe
Eyeshields, Gloves, type ABEK (EN14387) respirator filter
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E Salih et al.
The Journal of biological chemistry, 268(1), 245-251 (1993-01-05)
Acetylcholinesterase (AcChE, EC 3.1.1.7) was isolated from the electric organ of T. nobiliana and treated with the active-site-directed alkylating agent 1-bromo-2-[14C]pinacolone ([14C]BrPin), or with BrPin, which acts initially as a competitive inhibitor, Ki = 0.18 mM, and then inactivates the
S G Cohen et al.
Biochimica et biophysica acta, 997(3), 167-175 (1989-08-31)
1-Bromo-2-[14C]pinacolone, (CH3)3C14COCH2Br [( 14C]BrPin), was prepared from [1-14C]acetyl chloride and tert-butylmagnesium chloride with cuprous chloride catalyst, followed by bromination. It was examined as an active-site directed label for acetylcholinesterase (acetylcholine acetylhydrolase, EC 3.1.1.7) (AcChE). AcChE, isolated from Torpedo nobiliana, has
E Salih et al.
Biochimica et biophysica acta, 1208(2), 324-331 (1994-10-19)
To characterize the structure of the active site of acetylcholinesterase (AChE) from the electric organ of E. electricus, we identified sites of incorporation of two active-site affinity labels, [3H]diisopropyl fluorophosphate ([3H]DFP), and 1-bromo-2-[14C]pinacolone ([14C]BrPin). AChE was isolated, purified, inactivated and