STUDIES ON PHYSICAL AND CHEMICAL MODIFICATION OF PROTEINS FOR THE PREVENTION OF IRRADIATION OFF-FLAVORS IN MEAT

Abstract

Radiation damage to ovalbumin, hemoglobin and cytochrome c has been studied under anaerobic condition and the degradation mechanisms are discussed. The radio-lability of free amino acids was determined and evaluation methods for the radio-lability are discussed. The radio lability of amino acids as free amino acids or bound in peptide linkage in protein is also discussed. The radio-lability of methionine and its derivatives were studied and the degradation mechanisms are discussed. Decrease of radiation damage to ovalbumin, hemoglobin and cytochrome c by cystine, AET and MEA was studied and their protection mechanisms are discussed. Decrease of radiation damage to some of the typical amino acids by methionine was studied and their mechanisms are discussed.

Open PDF

Document Details

Document Type
Technical Report
Publication Date
Sep 14, 1962
Accession Number
AD0407411

Entities

People

  • A. L. Tappel
  • F. Shimazu
  • K. S. Ambe
  • R. J. Romani
  • U. S. Kumta

Organizations

  • University of California

Tags

Communities of Interest

  • C4I
  • Ground and Sea Platforms

DTIC Thesaurus Topics

  • Albumins
  • Amines
  • Amino Acids
  • Chemical Synthesis
  • Chemistry
  • Cyclic Amino Acids
  • Ionizing Radiation
  • Methionine
  • Sulfur
  • Sulfur Amino Acids
  • Sulfur Compounds

Readers

  • Analytical Chemistry
  • Molecular and Cellular Biochemistry
  • Nuclear and Radiation Engineering.