Molecular mass (kd) 145- 102- 75- 43- 27- [DTT] (MM) 10.00 1 2 3 4 5 6 Samples Questions 1. How many polypeptides are present in C3c? Determine their molecular masses from the figure. What was the purpose of using DTT in this experiment? What kind of bonds hold the polypeptides 2. 3. together? 4. How is the 102 kd polypeptide related to the other polypeptide species?

Human Anatomy & Physiology (11th Edition)
11th Edition
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Author:Elaine N. Marieb, Katja N. Hoehn
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Chapter1: The Human Body: An Orientation
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Experiment
This experiment was designed to analyze the structure of a component (C3c protein) of the
complement system, which is involved in the immune response against microorganisms. Purified
C3c protein (molecular mass: 145 kd) was incubated in the presence of various concentrations of
the reducing agent dithiothreitol (DTT) and then subjected to electrophoresis in a sodium
dodecyl sulfate (SDS)-polyacrylamide gel. SDS disrupts noncovalent bonds and polypeptides
are separated by size during electrophoresis. The gel was stained with Coomassie Brilliant Blue,
a protein dye. The figure shows the molecular masses of intermediates and products generated by
DTT treatment.
Results:
Molecular
mass (kd)
145-
102-
75-
43-
27-
[DTT] (MM)
10.00
1 2 3 4 5 6 Samples
Questions
1.
How many polypeptides are present in C3c?
Determine their molecular masses from the
figure.
What was the purpose of using DTT in this
experiment?
What kind of bonds hold the polypeptides
2.
3.
together?
4. How is the 102 kd polypeptide related to the
other polypeptide species?
Transcribed Image Text:Experiment This experiment was designed to analyze the structure of a component (C3c protein) of the complement system, which is involved in the immune response against microorganisms. Purified C3c protein (molecular mass: 145 kd) was incubated in the presence of various concentrations of the reducing agent dithiothreitol (DTT) and then subjected to electrophoresis in a sodium dodecyl sulfate (SDS)-polyacrylamide gel. SDS disrupts noncovalent bonds and polypeptides are separated by size during electrophoresis. The gel was stained with Coomassie Brilliant Blue, a protein dye. The figure shows the molecular masses of intermediates and products generated by DTT treatment. Results: Molecular mass (kd) 145- 102- 75- 43- 27- [DTT] (MM) 10.00 1 2 3 4 5 6 Samples Questions 1. How many polypeptides are present in C3c? Determine their molecular masses from the figure. What was the purpose of using DTT in this experiment? What kind of bonds hold the polypeptides 2. 3. together? 4. How is the 102 kd polypeptide related to the other polypeptide species?
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