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Factors Affecting Cyanoborohydride Reduction of Aromatic Schiff’s Bases in Proteins

  • Leroy Chauffe
  • Mendel Friedman
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 86A)

Abstract

Reductive alkylation of bovine serum albumin (BSA) and wool by aromatic aldehydes and sodium cyanoborohydride has been investigated. The aldehydes used were chosen to allow convenient quantitative measurement of binding by ultraviolet spectroscopy. Alkylation of BSA occurred primarily at two highly reactive sites. Variation of time, pH, reactant concentration, and addition of urea had little effect on the extent of alkylation of BSA. However, more extensive alkylation was achieved in buffered aqueous dimethyl sulfoxide. The unusual reactivity of two γ-amino groups on the BSA molecule is attributed to closely placed lysine residues in the primary sequence rather than to favorable placement of unrelated, distant reactive centers. Similarly, only a few of the potentially available γ-amino groups of wool were observed to react.

Keywords

Aromatic Aldehyde Bovine Serum Albumin Molecule Sodium Cyanoborohydride Reductive Alkylation Pyridine Carboxaldehyde 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1977

Authors and Affiliations

  • Leroy Chauffe
    • 1
  • Mendel Friedman
    • 1
  1. 1.Agricultural Research Service, U. S. Department of AgricultureWestern Regional Research LaboratoryBerkeleyUSA

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