S. S. Sorrell

Miles, Harold

doi:10.1007/978-1-4612-0295-0_20

Cited by 2 publications

(3 citation statements)

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“…Where high or low variability was noted within a dilution or between serial dilutions the Poisson Heterogeneity test was applied. Where counts at two dilutions were acceptable, the larger number were counted where possible, the standard error being approximately equal to the square root of the number of colonies counted (Miles and Misra 1938). Correlation coefficients (Pearson) for the two sets of five measurements for each of the three organisms were +0.80, +0.69 and +0.83, thus the technique was reproducible.…”

Section: Validity Of Plate Countmentioning

confidence: 99%

“…Fan et al (1988) A viable count was chosen as a measure as only live organisms are capable of causing infection. The Miles and Misra technique (Miles and Misra 1938) of serial dilutions and drop counts was identified as the most accurate for organisms able to grow well on opaque media and enabled verification that colonies were of the original species inoculated with no contaminants.…”

Section: Studymentioning

confidence: 99%

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Central Venous Catheter Infection

2015

Encyclopedia of Trauma Care

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Section: Validity Of Plate Countmentioning

confidence: 99%

Section: Studymentioning

confidence: 99%

Central Venous Catheter Infection

2015

Encyclopedia of Trauma Care

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“…Both were expressed in E. coli in the same way as wild-type P450 BM3 and purified using a similar protocol [22]. T h e haem domain of chimaera I proved to be unstable relative to that of wild-type nNOS, purifying with around 80 yo of the haem in the cysteine-detached P420 form.…”

Section: Swapping the Reductase Domains Of Bacillus Megaterium 111 (Bmentioning

confidence: 99%

Control of electron transfer in neuronal NO synthase

Daff

Noble

Craig

et al. 2001

Biochemical Society Transactions

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T h e nitric oxide synthases (NOSs) are dimeric flavocytochromes consisting of an oxygenase domain with cytochrome P450-like Cys-ligated haem, coupled to a diflavin reductase domain, which is related to cytochrome P450 reductase. T h e NOSs catalyse the sequential mono-oxygenation of arginine to N-hydroxyarginine and then to citrulline and NO. The constitutive NOS isoforms (cNOSs) are regulated by calmodulin (CaM), which binds at elevated concentrations of free Ca2+, whereas the inducible isoform binds CaM irreversibly. One of the main structural differences between the constitutive and inducible isoforms is an insert of 40-50 amino acids in the FMN-binding domain of the cNOSs. Deletion of the insert in rat neuronal NOS (nNOS) led to a mutant enzyme which binds CaM at lower Ca2+ concentrations and which retains activity in the absence of CaM. In order to resolve the mechanism of action of CaM activation we determined reduction potentials for the F M N and FAD cofactors of rat nNOS in the presence and absence of CaM using a recombinant form of the reductase domain. T h e results indicate that CaM binding does not modulate the reduction potentials of the flavins, but appears to control electron transfer primarily via a large structural rearrangement. We

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S. S. Sorrell

Cited by 2 publications

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Central Venous Catheter Infection

Central Venous Catheter Infection

Control of electron transfer in neuronal NO synthase

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