BIOCHEMISTRY
9th Edition
ISBN: 2818440090622
Author: BERG
Publisher: MAC HIGHER
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Chapter 3, Problem 29P
Interpretation Introduction
Interpretation:
The polyacrylamide gels can be formed in the presence of changing percentages of acrylamide resulting in different pore sizes. The usefulness of different pore sizes should be determined.
Concept introduction:
SDS-PAGE gel is known as the sodium dodecyl sulfate PAGE. And PAGE is known as the polyacrylamide gel electrophoresis. It is a modification of polyacrylamide gel electrophoresis. It is an analytical technique in biochemistry for the division of charged molecules in mixtures that are based on their molecular masses present in an electric field.
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What reagents promote cross-linking between acrylamide and bisacrylamide to form
polyacrylamide gel?
When separated on a polyacrylamide gel, the procedure is abbreviated as SDS-PAGE (Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis). The technique is a standard means for separating proteins according to their molecular weight. The gels are neutral, hydrophilic, three-dimensional networks of long hydrocarbons cross-linked by methylene groups.
(Give the main two compounds responsible for the formation of the gels)
The following proteins were separated by SDS-PAGE in the presence of mercaptoethanol. Sketch the relative positions of the various polypeptides on the gel. Label the positive and negative ends of the gel.Protein A: 40 kDa single polypeptideProtein B: 80 kDa protein, made up of two subunits of molecular weight 20 kDa and 60 kDa, held together by noncovalent interactionsProtein C: 200 kDa protein, made up of four identical subunits (50 kDa each) linked together by disulfide bonds
Chapter 3 Solutions
BIOCHEMISTRY
Ch. 3 - Prob. 1PCh. 3 - Prob. 2PCh. 3 - Prob. 3PCh. 3 - Prob. 4PCh. 3 - Prob. 5PCh. 3 - Prob. 6PCh. 3 - Prob. 7PCh. 3 - Prob. 8PCh. 3 - Prob. 9PCh. 3 - Prob. 10P
Ch. 3 - Prob. 11PCh. 3 - Prob. 12PCh. 3 - Prob. 13PCh. 3 - Prob. 14PCh. 3 - Prob. 15PCh. 3 - Prob. 16PCh. 3 - Prob. 17PCh. 3 - Prob. 18PCh. 3 - Prob. 19PCh. 3 - Prob. 20PCh. 3 - Prob. 21PCh. 3 - Prob. 22PCh. 3 - Prob. 23PCh. 3 - Prob. 24PCh. 3 - Prob. 25PCh. 3 - Prob. 26PCh. 3 - Prob. 27PCh. 3 - Prob. 28PCh. 3 - Prob. 29PCh. 3 - Prob. 30PCh. 3 - Prob. 31P
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- What is the practical advantage of the approximate red cell suspension over the exact red cell suspension?arrow_forwardWhat types of macromolecules are usually separated on agarose electrophoresis gels?arrow_forwardWhat is the difference of measuring proteins through UV-VIS spectroscopy at 280 nm and at 595 nm with the presence of the Bradford reagent? (note: explain not less than 5 sentences).arrow_forward
- You have 10 mg/ml ethidium bromide solution. If you add 5 µl of this to 50 ml of agarose gel solution, what will be the final concentration of ethidium bromide in the gel solution in mg/ml?arrow_forwardIf equal portions of tretinoin gel, 0.1 % w/w and 0.4 % w/w are combined, what would be the resultant percentage strength?arrow_forwardIn a mixture of five proteins listed, draw an elution profile (Absorbance vs. mL eluted, arbitrary) for the purification of the listed proteins on a gel filtration chromatography resin: cytochrome c (pI = 5.4; Mr = 13,000), immunoglobulin G (pI = 7.3; Mr = 145,000), ribonuclease A (pI = 9.6; Mr = 13,700), RNA polymerase (pI = 6.3; Mr = 450,000), human serum albumin (pI = 5.4; Mr = 68,500). Label your elution peaks. Draw a sketch of an SDS-PAGE, reflecting the mobility of the above mixture as they elute from the column. Label you protein bands.arrow_forward
- On an SDS-gel, If the distance traveled by the bromophenol blue dye is 7 cm, and the distance traveled by the protein band is 2.1 cm, the mobility of the protein is 0.3 30 3 30%arrow_forwardplease explain The porosity of the PAGE gel is determined by the ratio of acrylamide and the amount of .............................. (TEMD, bis-acrylamide, SDS, Glycine, Coomassie blue, iodocetate acetate, His tag, ammonium persulfate)arrow_forwardA mixture containing aspartic, lysine, serine and tyrosine was subjected to gel electrophoresis at pH 7.0. Indicate the position of each amino acid in the gel. (Show comprehensive explanation, and with graphical illustration if possible).arrow_forward
- Gradient PAGE uses differing gel concentrations along the length of the gel to achieve optimalseparation of proteins of a wide range of molecular weight proteins. How does the staining pattern of these types of gels differ from nongradient PAGE?arrow_forwardOwing to their structural similarity, separation of mixtures of organic compounds (such as the isomers 1-t- butyl-, 3-t-butyl-, and 4-t-butylcyclohexene) often proves difficult. Silica gel chromatography, however, can be used with some success provided that sufficient silica gel is used to provide optimal separation. Consider, for example, the TLC plate pictured at right after developing and UV visualization where prior to elution, lanes A and B were spotted with 1-t-butylcyclohexene and lanes B and C spotted with 4-t- butylcyclohexene. Which of the following must be true? In the space provided, indicate the CORRECT answers (as 1, 2, and/or 3) then explain your reasoning for all three statements. 1. 1-t-butylcyclohexene elutes faster than 4-t-butylcyclohexene. 2. The R; for both 1-t-butylcyclohexene and 4-t-butylcyclohexene are equal. 3. 4-t-butylcyclohexene is less polar than 1-t-butylcyclohexenearrow_forwardDefine about sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE)? Explain importance of sodiumdodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) ?arrow_forward
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