The branch of science concerned with chemical and physicochemical processes and substances present in living organisms. Say no to plagiarism. Get a tailor-made essay on “Why Violent Video Games Should Not Be Banned”? Get the original essay Biochemical analytical techniques refer to a set of methods, analyzes and procedures that allow scientists to study substances found in living organisms and chemical reactions. essential life processes. The more complex techniques are reserved for specialized research and diagnostic laboratories, while simplified sets of these techniques are used in common procedures such as screening for banned drug abuse at competitive sporting events and monitoring blood glucose in diabetic patients. List of biochemical techniques: Biochemical laboratory methods, systematic and analytical methods. It is an analytical technique dealing with the separation of closely associated compounds from a mixture. These consist of proteins, peptides, amino acids, lipids, carbohydrates, vitamins and drugs.Principles and categorizationChromatography generally consists of a mobile phase and a stationary phase.Mobile phase: The mobile phase refers to the combination of substances (to be separated), dissolved in a liquid or gas. Stationary phase: The stationary stage is a porous solid matrix through which the sample contained in the mobile phase percolates. Contact between the mobile and stationary phases causes the compounds in the mixture to separate. These interactions include physicochemical principles, for example adsorption, partitioning, ion exchange, molecular sieving and affinity. The interaction between stationary phase and mobile phase is frequently used in classification chromatography, e.g. partitioning, adsorption, ion exchange. In addition, the categorization of chromatography is also based either on the nature of the stationary phase (paper, thin layer, column) or on the nature of the mobile and stationary phases (gas-liquid chromatography). Electrophoresis: The movement of charged particles (ions) in an electric field resulting in their migration towards the electrode of opposite charge is called electrophoresis. Molecules with a net positive charge (cations) move toward the negative cathode while those with a net negative charge (anions) move toward the positive anode. Electrophoresis is a widely used analytical method for the separation of biological molecules, e.g. plasma proteins, lipoproteins and immunoglobulins. Types of electrophoresis: Electrophoresis zone Immunoelectrophoresis: Isoelectric focusing: Photometry: Photometry largely deals with learning the phenomenon of absorption of light by particles in solution. The specificity of a compound to capture light at a particular wavelength (monochromatic light) is exploited in the laboratory for quantitative measurements. Colorimeter: The colorimeter (or photoelectric colorimeter) is the tool used for measuring colored substances. This device operates in the observable range (400-800 nm) of the electromagnetic spectrum of light. The operation of the colorimeter is based on the principle of the Beer-Lambert law. The colorimeter generally contains a light source, a filter sample holder and a detector with display (counter or digital). A garland lamp usually serves as a light source. Filters allow a tiny range of wavelengths to pass through as incident light.Spectrophotometer: The spectrophotometer mainly differs from the colorimeter in covering the ultraviolet region (200-400 nm) of the electromagnetic spectrum. In addition, the spectrophotometer is more complicated with manydevices that ultimately increase the sensitivity of its operation several times compared to a colorimeter. A precisely selected wavelength (234 nm or 610 nm) in the ultraviolet and visible range can be used for measurements. Instead of glass cuvettes (in the colorimeter), quartz cells are used in a spectrophotometer. The spectrophotometer has basic elements similar to those described for a colorimeter. Ultracentrifugation: Ultracentrifugation is an essential instrument for the isolation of subcellular organelles, proteins and nucleic acids. Additionally, this technique is also used to determine the molecular weight of macromolecules. The rate at which sedimentation occurs during ultracentrifugation is based primarily on the mass and shape of the particles or macromolecules (i.e., molecular weight). It is expressed in terms of sedimentation coefficients).Centrifugation: Centrifugation is the use of centrifugal forces generated in a rotating rotor to divide biological particles. It includes cells, viruses, subcellular organelles, macromolecules (mainly proteins and nucleic acids) and macromolecular complexes (such as ribonucleoproteins and lipoproteins). The three main separation procedures are differential granulation, zonal centrifugation, and isopycnic centrifugation. The first two methods separate particles primarily on the basis of their volume, while isopycnic centrifugation separates particles based on their density. The choice of centrifugation technique depending on the nature of the particles and often above a separation technique is mandatory. For example, membrane fractionation often involves first producing an enriched fraction from a cell homogenate by Differential pelleting followed by isopycnic nuclear magnetic resonance: Nuclear Magnetic Resonance (NMR) spectroscopy is an analytical chemistry method used in quality control and research to determine the content and purity of a test with its molecular structure. Centrifugation to obtain purified fractions. Mass Spectrometry: Mass spectrometry is a useful analytical technique used to quantify known materials, identify unidentified compounds in a sample, and elucidate the structure and chemical properties of different molecules. The entire process involves transforming the sample into gaseous ions, with or without fragmentation, which are then characterized by their mass/charge (m/z) ratios and relative abundances. This method mainly studies the effect of ionizing energy on molecules. It is based on gas-phase chemical reactions in which sample molecules are consumed in the formation of ionic and neutral species. Principle: The initial step in the mass spectrometric analysis of compounds is the manufacture of ions in the gas phase of the compound, mainly by electronic ionization. . This molecular ion undergoes fragmentation. Each primary product ion derived from the molecular ion in turn undergoes fragmentation, and so on. Ions are separated in the mass spectrometer based on their mass-to-charge ratio and are detected in proportion to their large quantity. A mass spectrum of the molecule is thus formed. It displays the result as a plot of ion abundance versus mass-to-charge ratio. THE.