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Chemical Deterioration of Proteins by John R. Whitaker and Masao Fujimaki (Eds.)

By John R. Whitaker and Masao Fujimaki (Eds.)

content material: review at the chemical deteriorative adjustments of proteins and their effects / Robert E. Feeney --
Posttranslational chemical amendment of proteins / Rosa Uy and Finn Wold --
Chemical alterations in elastin as a functionality of maturation / Robert B. Rucker and Michael Lefevre --
Photooxidative harm to mammalian cells and proteins via seen gentle / L. Packer and E.W. Kellogg, III --
Chemical deterioration of muscle proteins in the course of frozen garage / Juichiro J. Matsumoto --
renovation of enzymes through conjugation with dextran / J. John Marshall --
adjustments occuring in proteins in alkaline resolution / John R. Whitaker --
Amino acid racemization in alkali-treated meals proteins : chemistry, toxicology, and dietary results / Patricia M. Masters and Mendel Friedman --
Deterioration of nutrition proteins via binding undesirable compounds resembling flavors, lipids and pigments / Soichi Arai --
Deteriorative adjustments of proteins in the course of soybean foodstuff processing and their use in meals / Danji Fukushima --
Suicide enzyme inactivators / Brian W. Metcalf.

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55. Masters, P. , this publication. 56. Nashef, A. ; Osuga, D. ; Feeney, R. E. Anal. , 1977, 79, 394. 57. Rucker, R. ; Tinker, D. Intern. Rev. Exper. , 1977, 17, 1. 58. Rucker, R. , this publication. 59. ; Sadnik, I. Fed. , 1979, 38, 1979. 60. Bada, J. L . ; Kvenvolden, Κ. ; Peterson, E. Nature, 1973, 245, 308. 61. Masters, P. ; Zigler J S. Jr Nature 1977, 268, 71. 62. Bada, J. L . ; Schroeder, , , 62, 71. 63. , Adv. Chem. Series, 1979, in press. 64. Matsumoto, J. , this publication. 65. , this publication.

In chemical d e t e r i o r a t i o n s which occur i n a d v e r t e n t l y o r " n a t u r a l l y " , however, r e v e r s i b i l i t y i s u s u a l l y hard to a t t a i n . An example o f one t h a t i s o f a prac­ t i c a l nature i s the o x i d a t i o n o f the t h i o ether o f methionine to the s u l f o x i d e ( F i g u r e 5 ) . This type o f r e a c t i o n could be en­ countered i n the use o f hydrogen peroxide as a s t e r i l i z i n g agent. This r e v e r s i b i l i t y i s e a s i l y achieved by treatment w i t h low concentrations o f a reducing agent.

FEENEY Deteriorative Changes and Their Consequences Figure 19. A model for the anion- and iron-binding sites of transferrin depicted assuming an interlocking-site hypothesis. The protein furnishes five ligands to the metal in the iron binding site; three tyrosines and two histidines. The carbonate ion binds to an arginine in the anion-binding site and functions as a sixth ligand to the metal center. The carbonate forms a bridge between the metal- and the anion-binding sites in the active center (36).

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