Sulfhydryl and Disulfide Groups in Glycinin. The Major Soybean Protein.

Abstract

The number of disulfide (SS) bonds in Glycinin-the major soybean protein-and their rate of cleavage by dithiothreitol (DTT) were determined at various concentrations of urea. A progressive increase in SS bond scission was observed with increasing urea concentration reaching the maximum of 20 SS bonds at 8M urea. In addition, a linear relationship was obtained for the rate of SS cleavage as a function of urea concentration. These results indicate that most of the disulfide bridges are buried in the interior of the protein molecule. Upon exposure to alkaline denaturation, a maximum of 9.2 sulfhydryl (SH) groups were obtained per mole of glycinin at pH 11.9.

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Document Details

Document Type
Technical Report
Publication Date
Jan 01, 1977
Accession Number
ADA042461

Entities

People

  • Nicholas Catsimpoolas

Organizations

  • Massachusetts Institute of Technology

Tags

Communities of Interest

  • Ground and Sea Platforms

DTIC Thesaurus Topics

  • Acetic Acid
  • Acids
  • Alcohols
  • Amino Acids
  • Buffers (Chemistry)
  • Chemical Properties
  • Chemistry
  • Computers
  • Dermatologic Agents
  • Electrophoresis
  • Gel Electrophoresis
  • Ion Exchange
  • Measurement
  • Molecular Weight
  • Molecules
  • Peptides
  • Urea

Readers

  • Molecular and Cellular Biochemistry