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The influence of mercaptoethanol on the apparent molecular weights of jojoba and standard proteins separated by porosity gradient gel electrophoresis in presence of urea
Author(s) -
Shah Akbar A.
Publication year - 1984
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150050316
Subject(s) - molecular mass , chemistry , chromatography , gelatin , electrophoresis , albumin , gel electrophoresis , 2 mercaptoethanol , urea , serum albumin , polyacrylamide gel electrophoresis , biochemistry , enzyme
Proteins 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.