Results 151 to 160 of about 3,639 (186)
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ω-Hydroxylation of acyclic monoterpene alcohols by rat lung microsomes

Biochemical and Biophysical Research Communications, 1982
Rat lung microsomes were shown to ω-hydroxylate acyclic monoterpene alcohols in the presence of NADPH and O2. NADH could neither support hydroxylation efficiently nor did it show synergistic effect. The hydroxylase activity was greater in microsomes prepared from β-naphthoflavone (BNF)-treated rats than from phenobarbital (PB)-treated or control ...
Chadha, Anju, Madyastha, KM
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Acyclic monoterpenes from the essential oil of Tagetes minuta flowers

Phytochemistry, 1998
Abstract The steam-distilled essential oil of T. minuta flowers afforded three new acylic monoterpene ketones identified as 3,7-dimethyloct-1-en-6-one, 3,7-dimethyl-5-hydroxyoct-1-en-6-one and 3,7-dimethyloct-1,7-dien-6-one along with major compounds ( Z )- β -ocimene (38.77%), dihydrotagetone (9.07%), ( Z )-tagetone (7%), ( Z )-ocimenone and ( E )-
S.N. Garg, V.K. Mehta
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Acyclic polyhalogenated monoterpenes from four marine hydroids

Biochemical Systematics and Ecology, 1984
Abstract Four polyhalogenomonoterpenes have been isolated from four species of marine hydroids. Their biological role is briefly discussed.
DE NAPOLI, LORENZO   +3 more
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Regiospecific hydroxylation of acyclic monoterpene alcohols by aspergillus niger

Tetrahedron Letters, 1988
Aspergillus niger was shown to carry out the regiospecific hydroxylation of acyclic monoterpene alcohols.
Madyastha, Madhava K   +1 more
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ChemInform Abstract: Microbial Hydroxylation of Activated Acyclic Monoterpene Hydrocarbons.

ChemInform, 1992
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.
W.‐R. ABRAHAM, H.‐A. ARFMANN
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Microbial transformations of acyclic monoterpenes

Proceedings / Indian Academy of Sciences, 1984
Microbial degradation of geraniol, citronellol, linalool and their corresponding acetates, structurally modified linalool and linalyl acetate, α-terpineol and β-myrcene are presented. Oxygenative and prototropic rearrangements are normally observed during the microbial metabolism of monoterpenes.
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Effect of acyclic monoterpene alcohols and their derivatives on TRP channels

Bioorganic & Medicinal Chemistry Letters, 2014
A series of thirty-six geraniol, nerol, citronellol, geranylamine, and nerylamine derivatives was synthesized and tested on TRPA1, TRPM8, and TRPV1 channels. Most of them acted as strong modulators of TRPA1 channels with EC50 and/or IC50 values
ORTAR, Giorgio   +5 more
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Role of acyclic compounds in monoterpene biosynthesis in Pinus pinaster

Phytochemistry, 1982
Abstract The biosynthesis of monoterpene hydrocarbons was studied in maritime pine needles by incorporation of 14CO2. It was shown that the acyclic terpenes β-myrcene and trans-β-ocimene, act as transitory compounds before the biosynthesis of cyclic monoterpenes such as α- and β-pinene. The mechanisms of biosynthesis are genetically controlled.
Michel Gleizes   +3 more
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Thienyl analogues of acyclic monoterpene alcohols and their biological activity

Journal of the Science of Food and Agriculture, 2009
AbstractBACKGROUND: Thienyl analogues of linalool, geraniol, nerol and citronellol were synthesised and their sensory and anti‐ microbial activities were investigated.RESULTS: The thienyl analogues of linalool, geraniol, nerol and citronellol, in which the isobutenyl moiety was replaced by a thiophene substituent, were synthesised from commercially ...
Radosław Bonikowski   +3 more
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Acyclic monoterpene primary alcohol:NADP+ oxidoreductase of Rauwolfia serpentina cells: the key enzyme in biosynthesis of monoterpene alcohols.

Journal of biochemistry, 1991
Acyclic monoterpene primary alcohol:NADP+ oxidoreductase, a key enzyme in the biosynthesis of monoterpene alcohols in plants, is unstable and has been only poorly characterized. However we have established conditions which stabilize the enzyme from Rauwolfia serpentina cells, and then purified it to homogeneity.
H, Ikeda   +6 more
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