Abstract
AbstractProteins exhibit higher apparent molecular weights when treated with mercaptoethanol and separated electropretically in a porosity gradient in presence of ureacompared to their apparent molecular weights without mercaptoethanol. This unexpected effect was first noticed with proteins of jojoba. The apparent increase was also seen when oligomers of serum albumin were separated, but was absent with gelatin, indicating a reaction of disulfide groups in the polypeptide chain of serum albumin. When the proteins were treated with hydrogen peroxide prior to electrophoresis the apparent increase of molecular weights of jojoba proteins after mercaptoethanol treatment was less evident in the presence of monomethylurea and was absent in gels containing tetramethylurea.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
