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Ovine and Bovine Metallothioneins: Purification, Number of Species, Zinc Content and Amino Acid Composition1

Philip D. Whanger, Sang-Hwan Oh2 and John T. Deagen

Department of Agricultural Chemistry, Oregon State University, Corvallis, OR 97331

Metallothioneins (MTs) were purified with respect to zinc from tissues of cattle and sheep which had been fed high levels of dietary zinc. These proteins were purified by gel filtration (Sephadex G-75), ion exchange chromatography (twice on DEAE Sephacel) and gel filtration again (Bio-Gel P-10). There is one major and up to three minor MT species in liver, kidney and pancreas from both sheep and cattle. The amount of zinc varies between the different species of MT. Amino acid analyses of the purified preparations revealed a cysteine content of up to 35.7% and the absence of aromatic amino acids for the major species, but the minor proteins contained less cysteine and some aromatic amino acids. The significance of MT in zinc metabolism is discussed.

KEY WORDS: • metallothionein • ovine • bovine

1 Published with the approval of the Oregon State Agricultural Experiment Station as technical paper no. 5687. This work was supported by Public Health Service Research Grant no. AM 19285 from the National Institute of Arthritis, Metabolism and Digestive Disease. This is the 10th paper of a series on the biological function of metallothionein.

2 Present address: Department of Biochemistry, College of Medicine, Yonsei University, P.O. Box 71, Seoul, Korea.

Manuscript received 12 December 1980.




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