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品質水準
アッセイ
98%
形状
crystals
bp
168-172 °C (lit.)
mp
93-96 °C (lit.)
SMILES記法
O=C1C[C@@H]2CC[C@H]1C2
InChI
1S/C7H10O/c8-7-4-5-1-2-6(7)3-5/h5-6H,1-4H2/t5-,6+/m1/s1
InChI Key
KPMKEVXVVHNIEY-RITPCOANSA-N
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適用法令
試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。
消防法
第2類:可燃性固体
引火性固体
危険等級III
Jan Code
N32601-25G:
N32601-BULK:
N32601-100G:
N32601-5G:
N32601-VAR:
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M B Bass et al.
Proteins, 13(1), 26-37 (1992-05-01)
While cytochrome P-450cam catalyzes the hydroxylation of camphor to 5-exo-hydroxycamphor with 100% stereospecificity, norcamphor is hydroxylated by this enzyme yielding 45% 5-exo-, 47% 6-exo-, and 8% 3-exo-hydroxynorcamphor (Atkins, W.M., Sligar, S.G., J. Am. Chem. Soc. 109:3754-3760, 1987). The present study
J R Collins et al.
The Journal of biological chemistry, 263(7), 3164-3170 (1988-03-05)
The hydroxylations of d-camphor, norcamphor, pericyclocamphanone, and 5,5-difluorocamphor by cytochrome P-450cam have been examined using theoretical methods to identify and characterize properties which determine product specificity. Experimental results indicate that each molecule is hydroxylated with quite different regio-specificity when metabolized
P J Loida et al.
The Journal of biological chemistry, 270(10), 5326-5330 (1995-03-10)
The stereoselectivity of cytochrome P450cam hydroxylation has been investigated with the enantiomerically pure substrate analog norcamphor. (1R)- and (1S)-norcamphor (> 92 enantiomeric excess) were characterized in the hydroxylation reaction with cytochrome P450cam with respect to the product profile, steady state
Megan C Thielges et al.
The journal of physical chemistry. A, 115(34), 9714-9723 (2011-06-09)
Progress in the field of 2D IR vibrational spectroscopy has been bolstered by the production of intense mid-IR laser pulses. As higher-energy pulses are employed, a concomitant increase occurs in the likelihood of fifth-order contributions to the 2D IR spectra.
J Contzen et al.
Biochemistry, 37(13), 4317-4324 (1998-04-29)
Step-scan time-resolved Fourier transform infrared spectroscopy with a time resolution of 5 micros was applied to the carbon monoxide complex of cytochrome P-450cam (CYP101) to study the bimolecular ligand-rebinding process after flash photolysis. Spectral changes in the CO ligand stretch
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