Micelles of pyridoxal-5′-phosphate Schiff bases - An improved model for the B6 site of glycogen phosphorylase

Abraham Kupfer, Viviane Gani, Shmuel Shaltiel

Research output: Contribution to journalArticlepeer-review


The spectral properties of Schiff bases obtained by reaction of pyridoxal-5′-P with n-alkylamines (CnNH2) at neutral pH depend upon the length of the hydrocarbon chain of the amine. While short-chain amines (e.g. n = 4,8) yield a product with absorption maxima at 405 and 273 nm (similar to those reported for pyridoxal-5′-P Schiff bases in an aqueous medium), higher members in the n-alkylamine series (e.g. n = 12), which form micelles under the conditions of the experiment, yield a product with absorption maxima at 335 and 252 nm, similar to those of Schiff bases in apolar solvents. Mixed micelles composed of hexadecyltrimethylammonium bromide and n-dodecylamine hydrochloride were found to entrap stoichiometric amounts of pyridoxal-5′-P (one mole per mole of the primary amine) and to yield a Schiff base. The resulting micelles simulate several absorption, fluorescence, and chemical properties of phosphorylase at neutral pH. This micellar model (like the functioning enzyme molecule) puts the pyridoxal-5′-P Schiff base in a hydrophobic microenvironment within an aqueous medium.

Original languageEnglish (US)
Pages (from-to)1004-1010
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - Dec 7 1977

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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