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33. Gel filtration chromatography shows that the molecular weight of a protein is 240,000 Daltons. However, when the protein was subjected to SDS-PAGE in the absence of ß- mercaptoethanol, two polypeptides (100,000 Daltons, 140,000 Daltons) were identified. Furthermore, when the protein was subjected to SDS-PAGE in the presence of ß- mercaptoethanol, three polypeptides (100,000 Daltons, 90,000 Daltons, and 50,000 Daltons were identified. Which of the following statements is true of the protein? A. The protein is composed of three polypeptides. B. The three-dimensional structure of the protein is stabilized by both covalent and non- covalent bonds. C. Both A and B. D. Neither A nor B. 34.What is purpose of SDS in SDS-PAGE? E. To selectively bind the target protein F. To maintain buffer pH in the gel G. To cause the separation of proteins to be on the basis of molecular weight only H. To initiate polymerization of acrylamide to form gel

33. Gel filtration chromatography shows that the molecular weight of a protein is 240,000 Daltons. However, when the protein was subjected to SDS-PAGE in the absence of ß- mercaptoethanol, two polypeptides (100,000 Daltons, 140,000 Daltons) were identified. Furthermore, when the protein was subjected to SDS-PAGE in the presence of ß- mercaptoethanol, three polypeptides (100,000 Daltons, 90,000 Daltons, and 50,000 Daltons were identified. Which of the following statements is true of the protein? A. The protein is composed of three polypeptides. B. The three-dimensional structure of the protein is stabilized by both covalent and non- covalent bonds. C. Both A and B. D. Neither A nor B. 34.What is purpose of SDS in SDS-PAGE? E. To selectively bind the target protein F. To maintain buffer pH in the gel G. To cause the separation of proteins to be on the basis of molecular weight only H. To initiate polymerization of acrylamide to form gel

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
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33. Gel filtration chromatography shows that the molecular weight of a protein is 240,000 Daltons. However, when the protein was subjected to SDS-PAGE in the absence of ß- mercaptoethanol, two polypeptides (100,000 Daltons, 140,000 Daltons) were identified. Furthermore, when the protein was subjected to SDS-PAGE in the presence of ß- mercaptoethanol, three polypeptides (100,000 Daltons, 90,000 Daltons, and 50,000 Daltons) were identified. Which of the following statements is true of the protein? A. The protein is composed of three polypeptides. B. The three-dimensional structure of the protein is stabilized by both covalent and non- covalent bonds. C. Both A and B. D. Neither A nor B. 34. What is purpose of SDS in SDS-PAGE? E. To selectively bind the target protein F. To maintain buffer pH in the gel G. To cause the separation of proteins to be on the basis of molecular weight only H. To initiate polymerization of acrylamide to form gel
Transcribed Image Text:33. Gel filtration chromatography shows that the molecular weight of a protein is 240,000 Daltons. However, when the protein was subjected to SDS-PAGE in the absence of ß- mercaptoethanol, two polypeptides (100,000 Daltons, 140,000 Daltons) were identified. Furthermore, when the protein was subjected to SDS-PAGE in the presence of ß- mercaptoethanol, three polypeptides (100,000 Daltons, 90,000 Daltons, and 50,000 Daltons) were identified. Which of the following statements is true of the protein? A. The protein is composed of three polypeptides. B. The three-dimensional structure of the protein is stabilized by both covalent and non- covalent bonds. C. Both A and B. D. Neither A nor B. 34. What is purpose of SDS in SDS-PAGE? E. To selectively bind the target protein F. To maintain buffer pH in the gel G. To cause the separation of proteins to be on the basis of molecular weight only H. To initiate polymerization of acrylamide to form gel
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