not easily extracted into the same 

 media. 



Katsuwonus pelamis (Linnaeus). 

 Experientia 10(4): 185-187. 



c. Oxymyoglobin was converted to metmyo- 

 globin on de-aeration. 



d. Stored meat showed evidence of progres- 

 sive denaturation of the pigment protein. 



4. The characteristics of the pigments of cooked 

 tunaflesh were investigated. One of the pig- 

 ments, denatured globin hemichrome, was 

 readily reduced to the hemochrome by chemi- 

 cal means. 



5. Evidence is presented showing a relation 

 between high metmyoglobin in the raw flesh 

 and a tendency towards discoloration on pre- 

 cooking, 



6. Data are cited indicating a low fat peroxide 

 content in normal meat relative to meat 

 inclined to become offcolor on precooking. 

 It is felt that fat oxidation and heme pigment 

 oxidation are interrelated. 



The conclusion reached is that greening 

 in tuna flesh is similar to the greening process 

 that occurs in other meats, and is due to an 

 anomalous heme protein oxidation. A hypothe- 

 tical pathway for the production of the green 

 condition in tuna flesh is outlined. 



LITERATURE CITED 



GINGER, 1. E., G. D. WILSON, and 

 B. S. SCHWEIGERT 



1954. Biochemistry of myoglobin. Quanti- 

 tative determination in beef and pork 

 muscle. Agri. and Food Chem. 2(20): 

 1037-1040. 



GINGER, I. E., U. J. LEWIS, and 

 B. S. SCHWEIGERT 



1955. Changes associated with irradiating 

 meat and meat extracts with gamma 

 rays. Agri. and Food Chem. 3(2): 

 156-159. 



KEILIN, D., and E. F. HARTREE 



1950. Reaction of methaemglobin with hydro- 

 gen peroxide. Nature 166(422 1): 513- 

 514. 



LEMBERG, R. , and J. W. LEGGE 



1949. Hennatin compounds and bile pigments. 

 New York: Interscience Publishers, 

 Inc. 748 p. 



LEWIS, U. J. 



1954. Acid cleavage of heme proteins. Jour. 

 Biol. Chem. 206(1): 109-120. 



MORGAN, V. E. 



1936. Studies on myoglobin. I. The solu- 

 bility of myoglobin in concentrated 

 ammoniunn sulfate solutions. Jour. 

 Biol. Chem. 112(2): 557-563. 



AUSTIN, J. H. , and D. L. DRABKIN 



1935-36. Spectrophotometric studies. III. 

 Methemoglobin. Jour. Biol. Chem. 

 112(1): 67-88. 



BOWEN, W. J. 



1949. The absorption spectra and extinction 

 coefficients of myoglobin. Jour. Biol. 

 Chem. 179(1): 235-245. 



BROWN, W. DUANE, and A. L. TAPPEL 



1957. Identification of the pink pigment of 

 canned tuna. Food Research 22(2) : 

 214-221. 



BRUCKMANN. G. , and S. G. ZONDEK 



1940. An improved method for the deter- 

 mination of nonhemin iron. Jour. 

 Biol. Chem. 135(1): 23-30. 



FOX, D. L. , and M. MILLOTT 



1954. A biliverdin-like pigment in the skull 

 and vertebrae of the ocecin skipjack. 



NAUGHTON, J. J., M. M. FRODYMA, and 

 H. ZEITLIN 



1956. Nature of green or offcolor condition 

 in precooked yellowfin tuna. U. S. 

 Fish and Wildlife Service, Spec. Sci. 

 Rept. — Fish. No. 197, 7 p. 



1957. Spectral reflectance applied t o the 

 study of heme pigments. Science 

 125(3238): 121-122. 



ROSSI-FANELLI, A,, and E. ANTONINI 



1955. Myoglobin and hemoglobin of sea 

 fishes. Crystallization and some 

 biochenaical properties, Congr. 

 intern, biochem. Resumes connmuns. 

 3 Congr. Brussels. (Chemical 

 Abstracts 50(5): 3659e. 1956). 



SHORLAND, F. B. 



1956. New trends in fats research. The 

 Austral. Jour, of Sci. 18(4A): 49-62. 



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