N-number: A protein has a molecular mass of 400 kDa when measured by size-exclusion dodecyl sulfate (SDS), the protein gives three bands with molecular masses of 180, chromatography. When subjected to gel electrophoresis in the presence of sodium 160, and 60 kDa. When electrophoresis is carried out in the presence of SDS and the reducing agent, dithiothreitol (DTT), three bands again form, this time with molecular masses of 160, 90, and 60 kDa. How many subunits does the protein have, and what is the molecular mass of each?
N-number: A protein has a molecular mass of 400 kDa when measured by size-exclusion dodecyl sulfate (SDS), the protein gives three bands with molecular masses of 180, chromatography. When subjected to gel electrophoresis in the presence of sodium 160, and 60 kDa. When electrophoresis is carried out in the presence of SDS and the reducing agent, dithiothreitol (DTT), three bands again form, this time with molecular masses of 160, 90, and 60 kDa. How many subunits does the protein have, and what is the molecular mass of each?
Chemistry
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ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
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Chapter1: Chemical Foundations
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![N-number:
dithiothreitol (DTT), three bands again form, this time with molecular masses of 160,
A protein has a molecular mass of 400 kDa when measured by size-exclusion
dodecyl sulfate (SDS), the protein gives three bands with molecular masses of 180,
chromatography. When subjected to gel electrophoresis in the presence of sodium
160, and 60 kDa.
When electrophoresis is carried out in the presence of SDS and the reducing agent,
dithiothreitol (DTT), three bands again form, this time with molecular masses of 160,
90, and 60 kDa.
How many subunits does the protein have, and what is the molecular mass of each?](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fb7c06261-a001-4995-9195-f7d1bc2aee2b%2F4685bc6a-7d45-4bbe-ba49-ac7e922fd0ce%2Ff4ksxhq_processed.jpeg&w=3840&q=75)
Transcribed Image Text:N-number:
dithiothreitol (DTT), three bands again form, this time with molecular masses of 160,
A protein has a molecular mass of 400 kDa when measured by size-exclusion
dodecyl sulfate (SDS), the protein gives three bands with molecular masses of 180,
chromatography. When subjected to gel electrophoresis in the presence of sodium
160, and 60 kDa.
When electrophoresis is carried out in the presence of SDS and the reducing agent,
dithiothreitol (DTT), three bands again form, this time with molecular masses of 160,
90, and 60 kDa.
How many subunits does the protein have, and what is the molecular mass of each?
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