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You have isolated a protein and use size exclusion chromatography to estimate its molecular mass to be 120 kDa. By SDS-PAGE you observe two bands at 80 kDa and 40 kDa. You can conclude that: This protein is a homodimer of 80 kDa subunits. This protein is a homotrimer of 40 kDa subunits. O The protein must contain disulphide bonds. The protein has degraded during SDS-PAGE. this protein consists of a heterodimer that contains 80 kDa and 40 kDa subunits.

You have isolated a protein and use size exclusion chromatography to estimate its molecular mass to be 120 kDa. By SDS-PAGE you observe two bands at 80 kDa and 40 kDa. You can conclude that: This protein is a homodimer of 80 kDa subunits. This protein is a homotrimer of 40 kDa subunits. O The protein must contain disulphide bonds. The protein has degraded during SDS-PAGE. this protein consists of a heterodimer that contains 80 kDa and 40 kDa subunits.

Human Anatomy & Physiology (11th Edition)
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
Section: Chapter Questions
Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
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You have isolated a protein and use size exclusion chromatography to estimate its molecular mass to be 120 kDa. By SDS-PAGE you observe two bands at 80 kDa and 40 kDa. You can conclude that: This protein is a homodimer of 80 kDa subunits. This protein is a homotrimer of 40 kDa subunits. O The protein must contain disulphide bonds. The protein has degraded during SDS-PAGE. this protein consists of a heterodimer that contains 80 kDa and 40 kDa subunits.
Transcribed Image Text:You have isolated a protein and use size exclusion chromatography to estimate its molecular mass to be 120 kDa. By SDS-PAGE you observe two bands at 80 kDa and 40 kDa. You can conclude that: This protein is a homodimer of 80 kDa subunits. This protein is a homotrimer of 40 kDa subunits. O The protein must contain disulphide bonds. The protein has degraded during SDS-PAGE. this protein consists of a heterodimer that contains 80 kDa and 40 kDa subunits.
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