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Alteration of porcine skeletal muscle myoglobin by the environment*

Published online by Cambridge University Press:  27 March 2009

N. W. Thomasf
Affiliation:
Purdue University, Department of Animal Sciences, Lafayette, Indiana 47907
M. D. Judge
Affiliation:
Purdue University, Department of Animal Sciences, Lafayette, Indiana 47907

Summary

Animals reared in constant ambient temperatures had significantly more skeletal muscle myoglobin than those reared in alternating temperature environments when the humidity was moderate or high. These differences did not exist when humidity levels were low. Comparisons ofthe effect of humidity level in constant ambient temperatures revealed high myoglobin in pigs subjected to moderate as compared to low humidity at 27°C, but humidity effects were nonexistent when the ambient temperature was 21 or 32° C. It is postulated that animals reared in alternating temperatures experienced intermittent and persistent development of tissue hypoxia and, asa consequence, had reduced aerobic metabolic pathways in muscle as compared to animals rearedinconstant ambient temperatures.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1970

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References

REFERENCES

Austin, J. H. & Drabkin, D. L. (1936). Spectrophotometric studies. III. Methemoglobin. Conversion of mefchemoglobin to cyano-methemoglobin. J. biol. Ohem. 112, 67.CrossRefGoogle Scholar
Briskey, E. J. (1964). Etiological status and associated studies of pale, soft, exudative porcine musculature. Adv. Fd Res. 13, 89.CrossRefGoogle Scholar
Brody, S. (1945). Bioenergetics and Growth. New York: Reinhold.Google Scholar
Dunoan, D. B. (1955). Multiple F tests. Biometrics 11, 1.Google Scholar
Forrest, J. C., Gundlach, R. F. & Briskey, E. J. (1963). A preliminary survey of the variations in certain pork ham muscle characteristics. Proc. Fifteenth Res. Conf. Circ. 74, 81.Google Scholar
Frankel, H. M., Ellis, J. P. Jr, & Cain, S. M. (1963). Development of tissue hypoxia during progressive hyperthermia in dogs. Am. J. Physiol. 201, 733.CrossRefGoogle Scholar
Ginger, I. D., Wilson, G. D. & Schweigert, B. S. (1954). Biochemistry of myoglobin. Quantitative determination of myoglobin in beef and pork muscle. Chemical studies of purified metmyoglobin. J. agric. Fd Ohem. 2, 1037.Google Scholar
Howe, J. M., Addis, P. B., Howard, R. D. & Judge, M. D. (1969). Environment-induced adrenocortical lipid in ‘stress-susceptible’ pigs. J. Anim. Sei. 28, 70.CrossRefGoogle Scholar
Howe, J. M., Thomas, N. W., Addis, P. B. & Judge, M. D. (1968). Temperature acclimation and its effect on porcine muscle properties in two humidity environments. J. Fd Sci. 33, 235.CrossRefGoogle Scholar
Huckabee, W. E. (1958a). Relationship of pymvate and lactate during anaerobic metabolism. I. Effects of infusion of pyruvate or glucose and of hyperventilation. J. din. Invest. 37, 244.Google Scholar
Huckabee, W. E. (1958b) Relationship of pyruvate and lactate during anaerobio metabolism. II. Exercise and formation of oxygen-debt. J. din. Invest. 37, 255.Google Scholar
Huckabee, W. E. (1958C). Relationship of pyruvate and lactate during anaerobic metabolism. III. Effect of breathing low-oxygen gases. J. din. Invest. 37, 264.Google Scholar
Judge, M. D., Briskey, E. J., Cassens, R. G., Forrest, J. C. & Meyer, R. K. (1968). Adrenal and thyroid function in ‘stress-susceptible’ pigs (Sus domesticus). Am. J. Physiol. 214, 146.CrossRefGoogle Scholar
Judge, M. D., Cahill, V. R., Kxtnkle, L. E. & Bnxraran, W. H. (1959). Pork Quality. I. Influences of some factors on pork muscle characteristics. J. Anim. Sci. 18, 448.CrossRefGoogle Scholar
Lawrie, R. A. (1950). Some observations on factors affecting myoglobin concentrations in muscle. J. agric. Sci., Camb. 40, 356.CrossRefGoogle Scholar
Li, J. C. (1965). Statistical Inference. I. Introduction to Statistical Inference. (2nd ed.). Ann Arbor: Edwards.Google Scholar
Needham, D. M. (1926). Red and white muscle Physiol. Rev. 6, 1.Google Scholar
NEiix, W. A. & Huckabee, W. E. (1966). Anaerobic heat production by the heart. J. din. Invest. 45, 1412.Google Scholar
Poel, W. E. (1959). Effect of anoxia on myoglobin concentration in striated muscle. Am. J. Physiol. 156, 44.CrossRefGoogle Scholar
Schweigert, B. S. (1954). Quantitative measurement of myoglobin. Proc. Seventh Ann. Recip. Meat Conf. 77.Google Scholar
Theorell, H. (1932). Kristallinisches myoglobin. I. Kristallisieren and reinigung des myglobais sowievorlaufige metteilung ttber sein molekulargewicht. Biochem. Z. 252, 1.Google Scholar