Ion Exchange chromatography: Ion exchange chromatography is a unique technique for effective separation of ions, amino acids, peptides, nucleotide and nucleic acids etc. This technique is widely used in the pre-fractionation or purification of a target protein from crude biological samples. It is used for separation of polar/charged/hydrophilic molecules. We can separate macromolecules like proteins, amino acid or nucleotides through ion chromatography. Mobile phase and liquid phase can be of different type i.e., it can be liquid, gas or solid but here Mobile phase is liquid and stationary phase is solid. Mainly the column chromatography is used for this purpose. Column chromatography means we construct columns of polymers like cellulose or …show more content…
1. Cation exchange chromatography 2. Anion exchange chromatography Cation exchange chromatography: In this type of chromatography stationary phase retains the cations. And here A- will be negatively charged which is masked by positively charged molecule B+. Mobile phase will have cations (say C+) which need to be separate. As the idea here is the exchange of ion. Negative part (A-) attached to the agarose is already attached to positive part (B+) so to remove B+ we need to add another negative part(D-) . It will help to remove B+ and in addition of C+ to A-. Then this desired cation C+ will be separated by Buffer solution. By using cation exchange chromatography we can separate proteins like lysine, arginine and histidine. Anion exchange chromatography: In this type of chromatography stationary phase retains the anion. Here A+ will be positively charged which is masked by a negatively charged molecule B-. Mobile phase will have anions (say C-) which need to be separate. As the idea here is also ion exchange. Positive part (A+) attached to agarose is already attached to negative part(B-) So to remove B we need to add another positive part (D+). It will help to remove B and in addition of C- to A+. Then desired anion (C-) will be separated by buffer solution. By using anion exchange chromatography we can separate proteins like aspartic acid and glutamic
The objective of this experiment was to perform extraction. This is a separation and purification technique, based on different solubility of compounds in immiscible solvent mixtures. Extraction is conducted by shaking the solution with the solvent, until two layers are formed. One layer can then be separated from the other. If the separation does not happen in one try, multiple attempts may be needed.
Cu (aq) + 2NO3 (aq) + 2Na+ (aq) + 2OH- (aq) → Cu(OH)2 (s) + 2Na+ (aq) + 2NO3(aq)
During this time, it could only be used in a lab with semi-intense supervision. Now, fast forward a few decades and there are D.I.Y. at home kits. The process of Electrophoresis starts with an electric current being run through a gel containing the molecules of interest. The molecules will then travel through the gel in different directions and speeds, based on their size and charge, allowing them to be separated from each other. Dyes, fluorescent tags, and radioactive labels can all enable the molecules on the gel to be seen after they have been separated. Because of these identification markers, they appear as a band across the top of the gel. Electrophoresis can be used for many different things. It is used to identify and study DNA or DNA fragments, and helps us to better understand the molecular components of both living and deceased organisms. Electrophoresis can also be used to test for genes related to specific diseases and life altering diagnoses such as Multiple Sclerosis, Down’s Syndrome, kidney disease, and some types of cancer. Electrophoresis also plays a major role in the testing of antibiotics. It can be used to determine the purity and concentration of one specific type of antibiotic or several general antibiotics at a time. Electrophoresis is also extremely useful in the creation and testing of
The equation shows how 1 mol of Na2CO3 reacts with 1 mol of H2SO4, so
The distance of the initial extract line to a pigment band was divided by the distance of the marked solvent front to the initial extract line both were measured in cm. The RF (relative to front) was calculated for each pigment band, indicating the travelled distance between the pigment and the front (solvent line) on the chromatography
We have to emphasize the importance of memorizing certain names and formulas and some prefixes and suffixes that are used in building a system of nomenclature. From there on, it is a matter of applying the system to different names and formulas you meet. The summary all the ideas that will be presented in this essay help you to learn the nomenclature system.
The procedure for this experiment can be found in Inorganic Chemistry Lab Manual prepared by Dr. Virgil Payne.
As explained by Saferstein “Chromatography is a means of separating and tentatively identifying the components of a mixtur... ... middle of paper ... ... ively place the suspect or perpetrator behind bars. Analyzing soil compounds can be measured by the levels of organic molecules including n-alkanes, fatty alcohols and fatty acids, which are all found in the waxy outer layer of plant matter (Geddes, 2008). It basically states that compounds can remain in the soil for thousands of years, which explains that each area being tested has its unique organic profile.
When introduced into an ionic solution, positively charged ions will be electrostatically attracted to the anode and the negatively charged ions will be electrostatically attracted to the cathode. This act of moving ions means that charges are able to move from anode to the cathode and complete the circuit. These moving ions are essentially the same as moving electrons (electricity). This process of putting electrodes into a solution, using a direct electric current (D.C.), and separating chemicals based on their charge is known as electrolysis
Stationary phase is of extreme importance in an HPLC analysis, as the chemical nature of the same and its compatibility with the analyte of interest is extremely significant for efficient separation. The most commonly used stationary phase is silica packed column which acts as a adsorbent. Each component in the sample interacts with these silica particles and gets eluted out in different time intervals. These silica columns may be of C14 or C18 type depending on the component of interest and also the columns themselves come in various dimensions each with a specific purpose of analysis.
Agarose gel electrophoresis separates molecules by to their size, shape, and charge. Biomolecules such as DNA, RNA and proteins, are some examples. Buffered samples such as glycerol and glucose are loaded into a gel. An electrical current is placed across the gel. The current moves the molecules towards the cathode or anode. The speed of the moving molecules depends on the size, shape, and charge. The properties of the gel will definitely affect the movement. Small molecules are expected to move easily and faster thru the pores.
Gel electrophoresis is used in a variety of settings, particularly in molecular biology. Besides being used to separate nucleic acids, such as DNA and RNA, gel electrophoresis is also employed to divide proteins (Gel Electrophoresis). According to research, electrophoresis is applied for the following reasons, "To get a DNA fingerprint for forensic pur...
Materials and Methods: An ion exchange chromatography column was obtained and set up for purification with the addition of 0.5 ml ion exchange matrix. 1 ml
is impossible to specify a single best method to carry out a given analysis in
The actual, theoretical, and percent yield of sodium chloride was found. Sodium Carbonate was mixed with hydrochloric acid and the liquid was boiled until there was nothing left. The result was the production of salt, or sodium chloride.