0
Want this question answered?
Be notified when an answer is posted
Add your answer:
Earn +20 pts
Hydrometers salinometers and refractometers are used to measure what a.pH b.salinity c.turbidity d.dissolved oxygen?
b. salinity All three can be used to measure the amount of salinity is a liquid sample. Hydrometers and refractometers can also be used to measure other concentrations such as sugar content.
The use of prism in laboratory?
Prisms are commonly used in laboratories to separate light into its constituent colors, known as a spectroscope. This is useful for determining the chemical composition of substances based on the unique pattern of colors they produce when exposed to light. Prisms are also used in refractometers to measure the refractive index of liquids, which can provide information about their concentration or purity.
What is a refractometer?
A refractometer is a measuring instrument used to determine the refractive index of a substance, which can provide information about the concentration or purity of a solution. It works by measuring how light is bent (refracted) as it passes through the substance. Refractometers are commonly used in industries such as food and beverage, pharmaceuticals, and gemology.
How can prospect sapphire is there any sapphire detector presnt in the world?
Well, isn't that a lovely question! Detecting sapphires in the ground can be quite a magical journey. While there may not be a specific "sapphire detector," geologists and gemologists use a variety of tools like refractometers, microscopes, and even their keen eyes to identify these precious gemstones. Remember, the real treasure is in the adventure of discovering these beautiful gems!
What are the names of locating agents used in chromatography?
Size-exclusion chromatography (SEC) is also known as gel permeation chromatography (GPC) or gel filtration chromatography and separates molecules according to their size (or more accurately according to their hydrodynamic diameter or hydrodynamic volume). Smaller molecules are able to enter the pores of the media and, therefore, molecules are trapped and removed from the flow of the mobile phase. The average residence time in the pores depends upon the effective size of the analyte molecules. However, molecules that are larger than the average pore size of the packing are excluded and thus suffer essentially no retention; such species are the first to be eluted. It is generally a low-resolution chromatography technique and thus it is often reserved for the final, "polishing" step of a purification. It is also useful for determining the tertiary structure and quaternary structure of purified proteins, especially since it can be carried out under native solution conditions. An expanded bed chromatographic adsorption (EBA) column for a biochemical separation process comprises a pressure equalization liquid distributor having a self-cleaning function below a porous blocking sieve plate at the bottom of the expanded bed, an upper part nozzle assembly having a backflush cleaning function at the top of the expanded bed, a better distribution of the feedstock liquor added into the expanded bed ensuring that the fluid passed through the expanded bed layer displays a state of piston flow. The expanded bed layer displays a state of piston flow. The expanded bed chromatographic separation column has advantages of increasing the separation efficiency of the expanded bed. Expanded-bed adsorption (EBA) chromatography is a convenient and effective technique for the capture of proteins directly from unclarified crude sample. In EBA chromatography, the settled bed is first expanded by upward flow of equilibration buffer. The crude feed, a mixture of soluble proteins, contaminants, cells, and cell debris, is then passed upward through the expanded bed. Target proteins are captured on the adsorbent, while particulates and contaminants pass through. A change to elution buffer while maintaining upward flow results in desorption of the target protein in expanded-bed mode. Alternatively, if the flow is reversed, the adsorbed particles will quickly settle and the proteins can be desorbed by an elution buffer. The mode used for elution (expanded-bed versus settled-bed) depends on the characteristics of the feed. After elution, the adsorbent is cleaned with a predefined cleaning-in-place (CIP) solution, with cleaning followed by either column regeneration (for further use) or storage. Reversed-phase chromatography (RPC) is any liquid chromatography procedure in which the mobile phase is significantly more polar than the stationary phase. It is so named because in normal-phase liquid chromatography, the mobile phase is significantly less polar than the stationary phase. Hydrophobic molecules in the mobile phase tend to adsorb to the relatively hydrophobic stationary phase. Hydrophilic molecules in the mobile phase will tend to elute first. Separating columns typically comprise a C8 or C18 carbon-chain bonded to a silica particle substrate. Hydrophobic interactions between proteins and the chromatographic matrix can be exploited to purify proteins. In hydrophobic interaction chromatography the matrix material is lightly substituted with hydrophobic groups. These groups can range from methyl, ethyl, propyl, octyl, or phenyl groups. At high salt concentrations, non-polar sidechains on the surface on proteins "interact" with the hydrophobic groups; that is, both types of groups are excluded by the polar solvent (hydrophobic effects are augmented by increased ionic strength). Thus, the sample is applied to the column in a buffer which is highly polar. The eluant is typically an aqueous buffer with decreasing salt concentrations, increasing concentrations of detergent (which disrupts hydrophobic interactions), or changes in pH. In general, Hydrophobic Interaction Chromatography (HIC) is advantageous if the sample is sensitive to pH change or harsh solvents typically used in other types of chromatography but not high salt concentrations. Commonly, it is the amount of salt in the buffer which is varied. In 2012, Müller and Franzreb described the effects of temperature on HIC using Bovine Serum Albumin (BSA) with four different types of hydrophobic resin. The study altered temperature as to effect the binding affinity of BSA onto the matrix. It was concluded that cycling temperature from 50 to 10 degrees would not be adequate to effectively wash all BSA from the matrix but could be very effective if the column would only be used a few times. Using temperature to effect change allows labs to cut costs on buying salt and saves money. If high salt concentrations along with temperature fluctuations want to be avoided you can use a more hydrophobic to compete with your sample to elute it. [source] This so-called salt independent method of HIC showed a direct isolation of Human Immunoglobulin G (IgG) from serum with satisfactory yield and used Beta-cyclodextrin as a competitor to displace IgG from the matrix. This largely opens up the possibility of using HIC with samples which are salt sensitive as we know high salt concentrations precipitate proteins. Hydrodynamic chromatography (HDC) is derived from the observed phenomenon that large droplets move faster than small ones. In a column, this happens because the center of mass of larger droplets is prevented from being as close to the sides of the column as smaller droplets because of their larger overall size. Larger droplets will elute first from the middle of the column while smaller droplets stick to the sides of the column and elute last. This form of chromatography is useful for separating analytes by molar mass, size, shape, and structure when used in conjunction with light scattering detectors, viscometers, and refractometers. The two main types of HDC are open tube and packed column. Open tube offers rapid separation times for small particles, whereas packed column HDC can increase resolution and is better suited for particles with an average molecular mass larger than 10 5 {\displaystyle 10^{5}} daltons. HDC differs from other types of chromatography because the separation only takes place in the interstitial volume, which is the volume surrounding and in between particles in a packed column.HDC shares the same order of elution as Size Exclusion Chromatography (SEC) but the two processes still vary in many ways. In a study comparing the two types of separation, Isenberg, Brewer, Côté, and Striegel use both methods for polysaccharide characterization and conclude that HDC coupled with multiangle light scattering (MALS) achieves more accurate molar mass distribution when compared to off-line MALS than SEC in significantly less time. This is largely due to SEC being a more destructive technique because of the pores in the column degrading the analyte during separation, which tends to impact the mass distribution. However, the main disadvantage of HDC is low resolution of analyte peaks, which makes SEC a more viable option when used with chemicals that are not easily degradable and where rapid elution is not important. HDC plays an especially important role in the field of microfluidics. The first successful apparatus for HDC-on-a-chip system was proposed by Chmela, et al. in 2002. Their design was able to achieve separations using an 80 mm long channel on the timescale of 3 minutes for particles with diameters ranging from 26 to 110 nm, but the authors expressed a need to improve the retention and dispersion parameters. In a 2010 publication by Jellema, Markesteijn, Westerweel, and Verpoorte, implementing HDC with a recirculating bidirectional flow resulted in high resolution, size based separation with only a 3 mm long channel. Having such a short channel and high resolution was viewed as especially impressive considering that previous studies used channels that were 80 mm in length. For a biological application, in 2007, Huh, et al. proposed a microfluidic sorting device based on HDC and gravity, which was useful for preventing potentially dangerous particles with diameter larger than 6 microns from entering the bloodstream when injecting contrast agents in ultrasounds
How does refractometer works?
A refractometer is a laboratory or field device for the measurement of an index of .... Automatic refractometers do not only measure the refractive index, but offer a lot of ... Refractometers and refractometry explains how refractometers work.
How does a refractometer works?
There are four main types of refractometers: traditional handheld refractometers, digital handheld refractometers, laboratory or Abbe refractometers, and inline process refractometers. There is also the Rayleigh Refractometer used (typically) for measuring the refractive indices of gases.In veterinary medicine, a refractometer is used to measure the total plasma protein in a blood sample and urine specific gravity.
Hydrometers salinometers and refractometers are used to measure what a.pH b.salinity c.turbidity d.dissolved oxygen?
b. salinity All three can be used to measure the amount of salinity is a liquid sample. Hydrometers and refractometers can also be used to measure other concentrations such as sugar content.
What type of Refractometer?
The refractive index of a substance indicates the degree to which it bends light that passes through it. A refractometer is an optical instrument that measures this parameter on any material. On obtaining this index, you can calculate different properties of the element, such as the concentration of blood protein, sugar content or salinity. Refractometers are classified into a few broad categories.Traditional Handheld RefractometersTraditional refractometers take advantage of the critical angle principle by which a shadow line is projected onto a tiny glass by prisms and lenses. The sample is placed between a small cover plate and a measuring prism. The point at which the shadow line crosses the scale indicates the reading. Automatic temperature compensation is a critical aspect of this refractometer, since the refractive index varies based on temperature.Digital Handheld RefractometersRevolutionizing the concept of refractometers, the digital handheld meters have been taking the scientific community by storm. They are compact, weigh little and have excellent water-resistant properties. Their tolerance for extremely high temperatures is an added advantage. The measurement times of these devices are in the range of two to three seconds, allowing almost instant measurements and working just as quickly as their handheld counterpartsLaboratory RefractometersFor researchers planning to measure multiple parameters and get the outputs in various formats, including printouts, these refractometers offer the perfect solution. They boast of a much wider range than that of handheld refractometers and a higher accuracy. The instruments' operations and measurement ranges can be programmed from remote computers as well, making laboratory refractometers more versatile.Inline Process RefractometersInline process refractometers save time and money. You can configure them to constantly collect specified statistics of the subject material remotely. The microprocessor control provides computer power that makes these devices very versatile.
What do mineralologists do?
Mineralogists use loupe eyepieces, refractometers, polariscopes, dichroscopes, hardness testers, streak testers, microscopes, tweezers, UV lighting, trays, brushes, cleaners, scales, calipers, and other tools of which the answerer is not aware.
What is a disadvantage of a refractometer?
Refractometers are used to measure the of a pure substance or mixture. Every has a unique refractive index that can be determined accurately. Refractive indices vary with composition as well as wavelengths of light, and are usually noted along with their respective wavelengths.
How does temperature affects measurement of brix?
Temperature can affect the measurement of Brix because refractometers are calibrated to give accurate readings at specific temperatures, usually at 20°C. If the temperature deviates from this calibration point, it can lead to inaccurate Brix readings. Temperature corrections can be applied to compensate for these variations and ensure accurate measurements.
The use of prism in laboratory?
Prisms are commonly used in laboratories to separate light into its constituent colors, known as a spectroscope. This is useful for determining the chemical composition of substances based on the unique pattern of colors they produce when exposed to light. Prisms are also used in refractometers to measure the refractive index of liquids, which can provide information about their concentration or purity.
What applications uses TIR?
Total internal reflection (TIR) is commonly used in optical devices such as fiber optics for telecommunications, endoscopes in medical imaging, and prisms in scientific instruments like spectrometers and laser systems. It is also utilized in sensor technologies like refractometers and biosensors for detecting changes in refractive indices.
How do you clean the refractometer?
To clean a refractometer, first wipe the prism with a soft cloth to remove any residue. Then, use a cleaning solution specifically designed for refractometers to gently clean the prism. Finally, rinse the prism with distilled water and dry it with a soft cloth before storing it in its case.
What is a refractometer?
A refractometer is a measuring instrument used to determine the refractive index of a substance, which can provide information about the concentration or purity of a solution. It works by measuring how light is bent (refracted) as it passes through the substance. Refractometers are commonly used in industries such as food and beverage, pharmaceuticals, and gemology.
How do you correct refractive index to 20 c?
To correct refractive index to 20°C from a different temperature, you can use the Gladstone-Dale equation or the Cauchy equation. These equations help adjust the refractive index for changes in temperature, ensuring accuracy in measurements. Alternatively, some refractometers come with automatic temperature compensation features that adjust the refractive index reading to a standardized temperature like 20°C.
