Spectroscopy. Behavioral Objectives: In order to attain this competency, the student should be able to:
Spectroscopy. 1. Turn on the instrument and lamp at least one hour prior to running samples
2. Check instrument dessicant and replace if necessary.
3. Run instrument diagnostics. Do not proceed until instrument passes all tests.
4. Run the QC sample each day at the beginning and end of each batch of samples.
5. Using a metal spatula, thoroughly mix the sample prior to removing a sample for spectroscopy. Avoid shaking the sample or any actin that cause the sample to separate by particle size.
6. Using a small scoop spatula, take four aliquots of material from different parts of the bag. Transfer each aliquot to a clean, dry Petri dish.
7. Close the Petri dish. Hold it by using your thumb on the cover and your middle finger at the base it (such as when holding a CD disk)and mix the material by shaking from left to right a couple of times. Avoid tapping or any action that causes the sample to separate by particle size.
8. Be careful at all times to avoid touching the Petri dish in areas within the spectroscopic window.
9. Make sure that your sample holder in the machine is free of any debris. Remove the top of the Petri dish and place only the base of your dish with the sample in it in the sample holder
10. Scan the sample using the instrument method provided. Repeat from ** until three spectra have been collected.
11. Average the three spectra and save the averaged spectrum. Only this spectrum will be forwarded to Ceres for analysis
Spectroscopy. In order to attain this competency, students should be able to:
Spectroscopy. During the fabrication of imprinted PV devices, P3HT, F8TBT and PCBM films were patterned by either or both XXXXX using chlo- roform (CHCl3) or dichloromethane (CH2Cl2) and/or NIL at an elevated temperature,
Spectroscopy. IN1 – Thermal TAS
Spectroscopy. Terminal oxidases are characterized by their optical absorp- tion spectra, reduced-minus-oxidized and CO-difference spectra, and by the EPR properties of their redox-sensitive prosthetic groups. The UV–visible light spectra of ‘Ca. M. oxyfera’ solubilized membranes showed Soret peaks at 413.5 and 432 nm, and bands at 535, 552 and 563 nm peaks in the a/b region (Fig. 2). Overall, the spectra showed all features of the bo-type oxidase purified from E. coli (Xxxxxx & Xxxxxxxx, 1984; Xxxxxxxxx & Xxxxxxxx, 1991). The Soret peaks at 413.5/432 nm in the CO-difference spectrum were very close to those of the E. coli enzyme (416/430 nm). Also, the positive peaks at 563/535 nm were similar to the E. coli Table 2. qRT-PCR characteristics and copy numbers of the subunits I of the three HCOs (HCO 1, HCO 2 and HCO 3), the AOX and the pMMO (pmoA) The negative controls were performed without cDNA. r2, Coefficient of determination. Gene Slope Efficiency (%) y Intercept r2 Negative control Copy number* HCO 1 3.29 99.2 40.91 0.998 2.626102 8.646105 HCO 2 3.20 96.5 39.17 0.999 2.026100 3.036103 HCO 3 3.44 103.9 41.99 0.999 5.756101 1.446106 AOX 3.26 98.4 41.24 0.996 1.086101 2.256105 pmoA 3.33 100.3 39.65 0.997 1.516103 6.856107 *Copy number per nanogram of total RNA.
