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Biomedical subjects

C Li

Publications and source records attributed to C Li.

At least 1,189 records · Page 66Linked to original sources
PubMed1989

The effects of changes in heart rate and aortic systolic pressure on left ventricular myocardial oxygen consumption in lambs.

To determine whether changes in heart rate and aortic systolic pressure contribute equally to the determination of left ventricular myocardial oxygen consumption, we independently varied heart rate and pressure and compared the resultant oxygen consumption for similar rate-pressure products. In 6 young lambs which underwent atrioventricular node ablation, we varied heart rate by ventricular pacing at 250 beats/min, 300 beats/min, and 120 beats/min while aortic pressure remained stable and varied aortic systolic pressure by infusion of phenylephrine (to 132 +/- 15 mm Hg and 155 +/- 14 mm Hg) and by infusion of sodium nitroprusside (to 79 +/- 6 mm Hg) while heart rate was maintained stable at 200 beats/min. The 3 levels of change in aortic systolic pressure were chosen so that the ratepressure product during the pressure changes matched the rate-pressure product during the heart rate changes. We found that left ventricular myocardial oxygen consumption was the same at all 3 levels of the rate-pressure product whether heart rate was changed and pressure remained stable or pressure was changed and heart rate remained stable. Also, the correlation between oxygen consumption and the rate-pressure product was similar for both heart rate and pressure changes. During nitroprusside infusion at a fixed heart rate, oxygen extraction was significantly lower than during pacing at a heart rate of 120 beats/min when the rate-pressure product was comparable because of the direct vasodilatory effects of nitroprusside. We conclude that heart rate and aortic systolic pressure contribute equally to left ventricular myocardial oxygen consumption at the same rate-pressure product, even though there may be differences in myocardial blood flow and oxygen extraction.

Animals↗
PubMed1988

Osmotaxis in Escherichia coli.

The escape of motile organisms from high concentrations of chemicals was studied in Escherichia coli. We have found all chemicals tested to be osmorepellents. It was shown in both a spatial assay and a temporal assay that the known sensory receptors for chemotaxis are not used for osmotaxis, so a different sensory mechanism appears to be employed. According to the temporal assay, the mechanism between sensory receptors and flagella is also not used for tumbling response (at least in solutions above 0.4 osmolar).

Chemotaxis↗
PubMed1988

Regulation of cardiac output with controlled heart rate in newborn lambs.

To determine the factors regulating cardiac output in newborn lambs and to examine the effects of age after birth, we altered heart rate, afterload, preload, and myocardial contractility in eight younger lambs, 5 to 13 days old, and seven older lambs, 15 to 36 days old. To control heart rate, we ablated the atrioventricular node by injecting formalin into the region of the node, and paced the right ventricle at a baseline heart rate of 200 beats/min. After the lambs recovered from surgery, we performed two protocols. In the first protocol we assessed the effects of changing heart rate by pacing the ventricle at various rates. We also examined the effect of altering afterload and preload at a fixed heart rate: afterload was increased by infusing phenylephrine and decreased by infusing nitroprusside. Preload was increased by infusing blood or 0.9% NaCl solution over 2 min. In the second protocol, we increased myocardial contractility by infusing isoproterenol at a fixed heart rate. Increasing heart rate above baseline levels caused no significant increase in cardiac output in the younger lambs (3.9 +/- 4.0%, mean +/- SD), and only small increases in the older lambs (11.4 +/- 6.7%). Decreasing heart rate, however, resulted in a progressive decrease in cardiac output in both groups of lambs. Decreasing afterload caused no significant increase in cardiac output in the younger lambs (1.4 +/- 14.0%) and only a small increase in the older lambs (11.1 +/- 1.9%).(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1987

Identification of three classes of hydrogenase in the genus, Desulfovibrio.

A comparison of amino-terminal amino acid sequences from the large and small subunits of hydrogenases from Desulfovibrio reveals significant differences. These results, in conjunction with antibody analyses, clearly indicate that the iron, iron + nickel, and iron + nickel + selenium containing hydrogenases represent three distinct classes of hydrogenase in Desulfovibrio.

Amino Acid Sequence↗
PubMed1987

Cloning of the 3'-phosphoadenylyl sulfate reductase and sulfite reductase genes from Escherichia coli K-12.

The structural genes for 3'-phosphoadenylyl sulfate (PAPS) reductase (cysH) and sulfite reductase (alpha and beta subunits; EC 1.8.1.2)(cysI and cysJ) of Escherichia coli K-12 have been cloned by complementation. pCYSI contains two PstI fragments (18.3 and 2.9 kb) which complement cysH-, cysI-, and cysJ- mutants. Subcloning showed that the cysH gene is located on a 1.6-kb ClaI subfragment (pCYSI-3) whereas cysI and most of cysJ are carried on a 3.7-kb ClaI subfragment (pCYSI-5). The PAPS reductase gene is closely linked to the sulfite reductase genes, but its expression is regulated by a unique promoter. The cysI and cysJ genes, on the other hand, are transcribed as an operon and the promoter precedes the cysI gene. Maxicell analysis demonstrated that pCYSI encodes three polypeptides of Mr 27,000, 57,000, and 60,000, in addition to the tetracycline-resistance determinant. The 60- and 57-kDa proteins are most likely the alpha and beta subunits, respectively, of E. coli sulfite reductase while the 27-kDa protein is putatively identified as PAPS reductase. Preliminary data suggest that the alpha and beta subunits of sulfite reductase are encoded by cysI and cysJ, respectively.

Chromosome Mapping↗
PubMed1987

Cloning, characterization, and sequencing of the genes encoding the large and small subunits of the periplasmic [NiFe]hydrogenase of Desulfovibrio gigas.

The structural genes for the large and small subunits of Desulfovibrio gigas periplasmic [NiFe]hydrogenase were identified and isolated by immunological and oligonucleotide screening. The gene for the small subunit codes for a 266-amino-acid, 28,724-dalton polypeptide which is separated by 63 nucleotides from the large subunit gene that codes for a 560-amino-acid, 61,707-dalton polypeptide. A putative signal peptide precedes the small subunit coding region, which may direct transport of the enzyme into the periplasmic compartment. Comparison of the amino acid sequence of this enzyme with those of two other classes of hydrogenase found in Desulfovibrio revealed that the D. gigas periplasmic hydrogenase has some homologies to the periplasmic [NiFeSe]hydrogenase of D. baculatus but none to the periplasmic [Fe]hydrogenase of D. vulgaris. The genes for the large and small subunits of the D. gigas hydrogenase hybridize strongly to genomic DNAs from several species of Desulfovibrio, indicating molecular similarity of the [NiFe]hydrogenase among sulfate reducers.

Amino Acid Sequence↗
PubMed1987

FMRFamide-like substances in the leech. III. Biochemical characterization and physiological effects.

FMRFamide-like immunoreactivity has been previously localized to identified neurons in the CNS of the leech, Hirudo medicinalis (Kuhlman et al., 1985a). These leech antigens have been characterized biochemically by reverse-phase high-pressure liquid chromatography (HPLC) followed by radioimmunoassay (RIA). The majority of the FMRFamide-like immunoreactivity recovered by HPLC from extracts of leech nerve cords coelutes with authentic FMRFamide. We have tentatively identified this major leech peptide as authentic FMRFamide. Two neurons that control heartbeat in the leech, the HE motor and HA modulatory neurons, and their neural processes on the heart are FMRFamide-like immunoreactive (Kuhlman et al., 1985a). Single individually dissected HE and HA cells were analyzed by HPLC and RIA. Only 1 FMRFamide-like peptide was found in extracts of HA cells; this peptide was chromatographically indistinguishable from authentic FMRFamide. The FMRFamide-like peptide in HE cells could not be isolated by experimental procedures used. Most of the FMRFamide-like immunoreactivity contained within the neural processes on the heart also coeluted with authentic FMRFamide. HE motor neurons, which are believed to be cholinergic (Wallace, 1981a, b; Maranto and Calabrese, 1984a, b), were examined for their FMRFamide-like effects on the heart. The presence of curare in the bathing medium did not block the ability of FMRFamide to induce myogenic activity in heart muscle, suggesting that FMRFamide and ACh act at different receptor sites on the heart. Prolonged firing in HE cells in the presence of curare also induced myogenic activity in heart muscle. This FMRFamide-like action of the HE motor neurons may be normally masked by their cholinergic actions.

Animals↗
PubMed1986

Complementation of an Escherichia coli pyrF mutant with DNA from Desulfovibrio vulgaris.

A PyrF- mutant of Escherichia coli (SK1108, pyrF::Tn5 Kanr) was complemented with the Desulfovibrio vulgaris (Hildenborough) structural gene for orotidine-5'-phosphate decarboxylase (EC 4.1.1.23). Either orientation of a 1.6-kilobase-pair D. vulgaris DNA fragment (pLP3B or pLP3A) complemented the PyrF- strain suggesting that the D. vulgaris pyrF promoter was functional. The apparent product of the D. vulgaris pyrF gene was a single 26-kilodalton polypeptide. These results demonstrate the utility of E. coli cloning systems in studying metabolic and energetic pathways in sulfate-reducing bacteria.

Carboxy-Lyases↗