Isolation and characterisation of porcine sorbin

Eur J Biochem. 1991 Oct 1;201(1):53-9. doi: 10.1111/j.1432-1033.1991.tb16254.x.


Sorbin has been isolated from extracts of porcine upper intestine, and the biological activity in absorbing water and electrolytes utilized to monitor the purification procedure. Pure sorbin was obtained in a yield of about 1 mg/Mg boiled intestine. The protein chain has 153 amino acid residues and the primary structure was determined by analyses of CNBr-cleaved fragments and four enzymatic digests. The protein has a free N-terminal Met and an amidated C-terminal Ala. No structural similarity was observed with other known proteins in data bases, but several segments have special properties and the C-terminal half is rich in Pro and Arg.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Absorption
  • Amino Acid Sequence
  • Amino Acids / analysis
  • Animals
  • Cyanogen Bromide
  • Gallbladder / drug effects
  • Gallbladder / metabolism
  • Guinea Pigs
  • Intestines / chemistry*
  • Molecular Sequence Data
  • Peptide Fragments / chemistry
  • Peptides / chemistry
  • Peptides / isolation & purification*
  • Peptides / pharmacology
  • Swine
  • Water / metabolism


  • Amino Acids
  • Peptide Fragments
  • Peptides
  • Water
  • sorbin peptide
  • Cyanogen Bromide