Reference

Methyl ketone formation by Penicillium camemberti in model systems

Methyl ketone formation by Penicillium camemberti in model systems. Okumura, J.; Kinsella, J. E. (Inst. Food Sci., Cornell Univ., Ithaca, NY 14853, USA). J. Dairy Sci., 68(1), 11-15 (English) 1985. CODEN: JDSCAE. ISSN: 0022-0302. DOCUMENT TYPE: Journal CA Section: 17 (Food and Feed Chemistry) Section cross-reference(s): 10 P. camemberti Incubated in a model system contg. milk lipids (45 mM) caused hydrolysis of the lipids with subsequent oxidn. of the free fatty acids to carbonyl compds. of which ~60% was composed of Me ketones, mainly of 2-nonanone [821-55-6] and 2-undecanone [112-12-9]. The addn. of lipase [9001-62-1] greatly enhanced carbonyl prodn. by the mycelium. Incubation in the presence of Na laurate [629-25-4] (45 mM) reduced mycelium growth, but extensive synthesis of undecanone occurred. The mycelium was more tolerant to exogenous oleic acid [112-80-1] and produced mostly heptanone [29299-43-2] and nonanone.

Anesthetic action of esters and ketones: evidence for an interaction with the sodium channel protein in squid axons

Anesthetic action of esters and ketones: evidence for an interaction with the sodium channel protein in squid axons. Elliott, J. R.; Haydon, D. A.; Hendry, B. M. (Physiol. Lab., Cambridge CB2 3EG, UK). J. Physiol. (London), 354, 407-18 (English) 1984. CODEN: JPHYA7. ISSN: 0022-3751. DOCUMENT TYPE: Journal CA Section: 1 (Pharmacology) The effects of methyl Bu ketone [591-78-6], methyl heptyl ketone [821-55-6] and methyl pentanoate [624-24-8] on the Na current of the squid giant axon have been examd. The peak inward current in intact axons was reduced reversibly by each substance. Shifts in the voltage dependence of the steady-state activation and inactivation parameters (m￥ and h￥), redns. in the peak heights of the activation and inactivation time consts. (tm and th) and changes in the max. Na conductance (gNa) caused by these substances have been tabulated and compared with the effects of methyl octanoate [111-11-5]. Each compd. shifted the voltage dependence of the steady-state inactivation parameter in the hyperpolarizing direction and that of the steady-state activation parameter in the depolarizing direction. The shifts produced by the ketones are compared with those produced by Me pentanoate and by Me octanoate. The possible role of an interaction between the carbonyl O of the test substance and the Na channel protein in producing the h￥ shift is discussed. The peak time consts. are reduced and the voltage dependences of tm and th are shifted in a direction commensurate with the shifts in steady-state properties. The max. Na conductance is not much affected either by the ketones or by Me pentanoate. This lack of a large effect on gNa indicates that whatever direct interaction does take place between the test substance and the channel protein, it does not result in a blockage of the channel.