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L Hibbard

Publications and source records attributed to L Hibbard.

6 recordsLinked to original sources
PubMed1991

Regional brain glucose metabolism is altered during rapid eye movement sleep in the cat: a preliminary study.

Glucose utilization was measured in 74 brain regions of the cat during states of wakefulness or rapid eye movement (REM) sleep. These data were obtained from intact, unanesthetized animals which were instrumented for objectively measuring states of consciousness. Through a chronically implanted intravenous catheter, the cats received 250 microCi of magnitude of 6-14C glucose during REM sleep (N = 3) or during wakefulness (N = 3). After spending approximately 8 min in REM sleep or in quiet wakefulness, the cats were administered a lethal dose of barbiturate and the brains were removed and processed for autoradiography. The results revealed site-specific changes in glucose metabolism during REM sleep. Significant alterations in glucose use occurred in the thalamus, the limbic system, and specific regions of the pontine reticular formation. These data demonstrate for the first time that during states comprised entirely of REM sleep there are anatomically specific changes in cerebral glucose metabolism. The majority of brain regions exhibiting REM sleep-dependent changes in glucose metabolism either overlapped with regions known to contain cholinergic cell bodies, or with areas that receive prominent cholinergic input.

Animals↗
PubMed1979

Isolation and characterization of single chain bovine factor V.

A procedure for the isolation of bovine Factor V has been developed. The Factor V is isolated from bovine plasma by a series of steps including barium citrate adsorption, polyethylene glycol precipitation, QAE-cellulose adsorption, hydrophobic chromatography on octyl Sepharose, ammonium sulfate fractionation, preparative electrophoresis on acrylamide gels, and finally, phenyl Sepharose chromatography. During isolation, judicious use of inhibitors including benzamidine hydrochloride, soybean trypsin inhibitor, and diisopropylphosphorofluoridate has been applied to prevent activation of the Factor V TO Factor Va. The activity of the isolated protein increases by a factor of 80 when stimulated by catalytic amounts of thrombin. The specific activity of the material after thrombin activation is 1250 units/mg of protein when evaluated versus a bovine Factor V standard in human factor V-deficient plasma. The isolated protein is a single component when analyzed by a variety of electrophoretic techniques and has been characterized in terms of its gross physical and chemical properties. Bovine Factor V is a single chain glycoprotein which has a molecular weight of 330,000. The single chain nature of the molecule has been established by sedimentation equilibrium studies of the native molecule and on the molecule in 6 M guanidinium chloride with and without disulfide bond reduction. In addition to these mass measurements, the single chain nature of the molecule has been established by hydrodynamic estimation of the random coil volume by sedimentation velocity studies of the reduced carboxyamidomethylated protein in 6 M guanidinium chloride. Native Factor V has a sedimentation coefficient so20,w of 9.19 S, which indicates the molecule is highly asymmetric. The frictional ratio f/fmin for the molecule is estimated to be 2.01, and the axial ratio of the equivalent prolate ellipsoid is 25:1. Thus, present data suggest that Factor V is a rod-like molecule composed of a single chain.

Amino Acids↗