Summary
The assignment of zinc bound to carbonic anhydrase isoenzymes (CA-I and CA-II) and Cu2 Zn2 superoxide dismutase (SOD1) was investigated in the hemolysates from 21 normal male subjects.
Sufficient care was taken to remove leukocytes and platelets. The following values of zinc distribution were obtained:total zinc, 1113.8±22.7 (mean±S.E.) μg · 100 ml−1; CA-I-derived zinc, 866.6±26.2 μg · 100 ml−1; CA-II-derived zinc, 99.9±3.9 μg · 100 m−1; SOD1-derived zinc, 60.3±1.9 μg · 100 ml−1; the other zinc, 87.0±12.6 μg · 100 ml−1. Namely, 7.6% of the zinc in human erythrocytes is not bound to the carbonic anhydrases and Cu2Zn2 superoxide dismutase, but present in available form or attached to other enzymes.
References
Beutler E, West C, Blume KG (1976) The removal of leukocytes and platelets from whole blood. J Lab Clin Med 88: 328–333
Bogden JD (1980) Blood zinc in health and disease. In: Nriagu JO (ed) Zinc in the environment, part II: health effects. Wiley, New York Chichester Brisbane Toronto, pp 137–169
Carrico RJ, Deutsch HF (1970) The presence of zinc in human cytocuprein and some properties of the apoprotein. J Biol Chem 245: 723–727
Dennes E, Tupper R, Wormall A (1962) Studies on zinc in blood. Transport of zinc and incorporation of zinc in leukocytes. Biochem J 82: 466–476
Funakoshi S, Deutsch HF (1970) Human carbonic anhydrase, III. Immunochemical studies. J Biol Chem 245: 2852–2856
Ishikawa N, Shiraishi T, Kondo T, Taniguchi N (1981) Zinc deficiency states and carbonic anhydrase isozyme in experimental hemolytic and bleeding anemia of rabbits. Enzyme 26: 85–92
Keilin D, Mann T (1939) Carbonic anhydrase. Nature 144: 442–443
Keilin D, Mann T (1940) Carbonic anhydrase. Purification and nature of the enzyme. Biochem J 34: 1163–1176
Mancini G, Carbonara AO, Heremans TF (1965) Immunochemical quantitation of antigen by single radial immunodiffusion. Immunochemistry 2: 235–254
Milunsky A, Hackley BM, Halsted JA (1970) Plasma, erythrocyte and leukocyte zinc levels in Down's syndrome. J Ment Defic Res 14: 99–104
Oelshlegel FJ jr, Brewer GJ, Prasad AS, Knutsen C, Schoomaker EB (1973) Effect of zinc on increasing oxygen affinity of sickle and normal red blood cells. Biochem Biophys Res Commun 53: 560–566
Ohno H, Hirata F, Terayama K, Kawarabayashi T, Doi R, Kondo T, Taniguchi N (1983) Effect of short physical exercise on the levels of zinc and carbonic anhydrase isoenzyme activities in human erythrocytes. Eur J Appl Physiol 51: 257–268
Rosner F, Gorfien PC (1968) Erythrocyte and plasma zinc and magnesium levels in health and disease. J Lab Clin Med 72: 213–219
Seino M (1976) Determination of erythrocyte zinc by atomic absorption spectrophotometry: its significance in iron deficiency anemia. Hokkaido J Med Sci 51: 59–72
Stansell MJ, Deutsch HF (1965) Preparation of crystalline erythrocuprein and catalase from human erythrocytes. J Biol Chem 240: 4299–4305
Stansell MJ, Deutsch HF (1965) Physicochemical studies of crystalline human erythrocuprein. J Biol Chem 240: 4306–4311
Swaminathan R, Segall NH, Chapman C, Morgan DB (1976) Red-blood-cell composition in thyroid disease. Lancet 2: 1382–1385
Taniguchi N, Sato T, Kondo T, Tamachi H, Saito K, Takakuwa E (1975) Carbonic anhydrase isozymes, hemoglobin-F and glutathione levels in lead-exposed workers. Clin Chim Acta 59: 29–34
Tashian RE (1977) Evolution and regulation of the carbonic anhydrase isoenzymes. In: Rattazzi MC, Scandadalios JG, White GS (eds) Isozymes; current topics in biological and medical research, vol 2. AR Liss, New York, pp 21–62
Wolff HP (1956) Untersuchungen zur Pathophysiologie des Zinkstoffwechsels. Klin Wochenschr 34: 409–418
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Ohno, H., Doi, R., Yamamura, K. et al. A study of zinc distribution in erythrocytes of normal humans. Blut 50, 113–116 (1985). https://doi.org/10.1007/BF00321175
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00321175