(ELECTROPHORESIS OF SERUM PROTEIN) DATE : 10 OCTOBER 2013 PART A SEPARATION OF SERUM PROTEINS USING THE ELECTROPHORESIS METHOD. OBJECTIVES: 1. To understand the analytical methods involved in analyzing serum proteins. 2. To study the serum protein electrophoresis pattern to aid the understanding of the relationship between the structure and the function of proteins. PRINCIPLE OF PRACTICAL: This technique is based on the movement of charged particles such as proteins when placed
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they can actually get to the places that they wish to visit via public transportation. In some countries‚ routes can be very limited‚ which can be a major disadvantage for travelers who do not have an alternative means of getting around. If a traveler does visit a place where the main attractions or accommodation options are not located near public transportation routes‚ he or she may need to inquire about private transportation services‚ such as taxi-cabs. Another consideration is that public transportation
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Diffusion and Osmosis lab Results: Figure 1a-rate of weight change in 15 min intervals of each concentration. The first tube showed very little weight change. However all other tubes show a greater change the concentration could be the factor that determines the permeability of the sucrose. The sucrose molecules are too large to pass through. Figure 1b- sucrose concentration determines the weight change. In this case based on our results as concentration increases the percent weight change
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Success comes from civic engagements. Civic engagements make a difference to society and individuals who are in need throughout a social structure. Social problems require civic engagement because civic engagement reduces the impact of a social problem through the promotion of a better quality of life. Civic engagements promote a better quality of life from framed principles‚ plans‚ and actions that contain a solution and a targeted outcome. The impact of a social problem is the possible recycled
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Protein powder is bad because it contained a lot of additive‚ sugar and too much protein. Although natural protein provide immune system defense for the body and also contain antioxidant components‚ however‚ that does not mean that protein shake or protein powder has the same function as the natural protein. As time goes by‚ protein powder has become essential for muscle builder to consume. People drink protein shakes or take pills while they are working out or after performing intense exercise.
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The purpose of this lab was to observe the rate of osmosis and diffusion‚ as well as the effect of molecular size of the particles on this rate. Part I of the lab was a demonstration of osmosis and diffusion‚ that dealt with raisins in different liquid environments‚ each with a different concentration of sugar. Part IV of the lab was using the same idea as the demonstration‚ by putting objects in different concentrations of a substance; in this case elodea leaves in salt water. In both cases‚ the
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If pH > pI‚ then the protein will have a negative charge and if pH < pI‚ the protein will have a positive charge. Buffer I has a pH >5‚ meaning both proteins carry a negative charge and bind to the DEAE (a positively charged resin). (b) pH = pKa + log10(Base/Acid) [Base = mM of sodium acetate; Acid = mM of acetic acid] = 4.7 + log10 (40/40) = 4.7 In order for the catalase to elute from the column‚ it must have lost its negative charge and stopped binding to the DEAE. Lowering the pH
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We successfully adapted a commercially available protein detection assay for the quantiWcation of PEI. All experiments described below were performed with linear 25-kDa PEI (Polysciences‚ Warrington‚ PA‚ USA) that we routinely use for the transfection of mammalian cells [4]‚ but it was possible to quantitate other PEIs (diVerent molecular weights; branched) with this method (data not shown). The mixing of a PEI solution with the Advanced Protein Assay (APA) reagent (Cytoskeleton‚ Denver‚ CO‚ USA)
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Expressing and Purifying the Recombinant form of Green Fluorescent Protein (rGFP) from the E.coli strain using Ni2+ agarose affinity chromatography technology Abstract The purpose of this experiment was to express and purify the his6-tagged recombinant form of GFP (rGFP) from the organism E.coli using Ni2+ agarose affinity chromatography. The expression of rGFP was confirmed qualitatively using the UV light and was expressed in the E.coli strain BL21 (DE3) (-- removed HTML --) (-- removed HTML
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Background: Pepsinogen is an inactive protein that is the mucus lining of the stomach. When converted to pepsin‚ the enzyme is used to break down large or undigested protein they has been absorbed by the small intestine. The digestive power of pepsin is greatest at the acidity of normal gastric juice (pH 1.5–2.5). In the intestine the gastric acids are neutralized (pH 7)‚ and pepsin is no longer effective. "Pepsin (biochemistry)." Encyclopedia Britannica Online. Encyclopedia Britannica‚ n.d. Web
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