Abstract
Multiple components of human α1-antitrypsin were separated by preparative starch gel electrophoresis, and the sialic acid contents of these components were determined. The acidic components contained more sialic acid per molecule than the basic components. The molecular sizes of these components were identical, excluding the possibility of polymerization of the inhibitor in the formation of the multiple components. Consequently, the multiple components of the inhibitor are primarily due to differences in the sialic acid content of each component. Three major components contain eight, seven, and six sialic acid residues per molecule, respectively.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Crawford, I. P. (1973). Purification and properties of normal human α1-antitrypsin. Arch. Biochem. Biophys. 156215.
Eriksson, S. (1963). Pulmonary emphysema alpha 1-antitrypsin deficiency. Acta Med. Scand. 175197.
Fagerhol, M. K. (1968). The Pi-system genetic variants of serum α1-antitrypsin. Ser. Haematol. 1153.
Hercz, A., and Barton, M. (1977). Partial preparative separation and properties of the isoinhibitors of human alpha 1-antitrypsin (alpha 1-protein inhibitor). Can. J. Biochem. 55661.
Kueppers, F. (1976). α1-Antitrypsin M: A new common genetically determined variant. Am. J. Hum. Genet. 28370.
Laurell, C. B., and Eriksson, S. (1963). The electrophoretic α1-globulin pattern of serum in α1-antitrypsin deficiency. Scand. J. Clin. Lab. Invest. 15132.
Lieberman, J. (1969). Heterozygous and homozygous alpha 1-antitrypsin deficiency in patients with pulmonary emphysema. New Engl. J. Med. 281279.
Lieberman, J., Gaidulis, L., and Garoutte, B. (1972). Identification and characteristics of the common alpha 1-antitrypsin phenotypes. Chest 62557.
Liu, T.-Y. (1972). Determination of sialic acid using an amino acid analyser. Methods Enzymol. 2848.
Mega, T., and Yoshida, A. (1978). Origin of the multiple components of human alpha 1-antitrypsin: Fed. Proc. 371337.
Musiani, P., Massi, G., and Piantelli, M. (1976). Separation of different molecular forms of serum alpha 1-antitrypsin. Clin. Chim. Acta 73561.
Owen, M. C., and Carrell, R. W. (1976). Alpha 1-antitrypsin: Molecular abnormality of S variant. Br. Med. J. 1130.
Sharp, H. L., Bridge, R. A., Krivit, W., and Freier, E. F. (1969). Cirrhosis associated with alpha 1-antitrypsin deficiency: A previously inherited disorder. J. Lab. Clin. Med. 73934.
Smithies, O. (1962). Molecular size and starch gel electrophoresis. Arch. Biochem. Biophys. Suppl. 1:125.
Warren, L. (1959). Thiobarbituric acid assay of sialic acids. J. Biol. Chem. 2341971.
Yoshida, A., Lieberman, J., Gaidulis, L., and Ewing, C. (1976). Molecular abnormality of human 1-antitrypsin variant (Pi-ZZ) associated with plasma activity deficiency. Proc. Natl. Acad. Sci. 731324.
Yoshida, A., Ewing, C., Wessels, M. Lieberman, J., and Gaidulis, L. (1977). Molecular abnormality of PiS variant of human alpha 1-antitrypsin. Am. J. Hum. Genet. 29233.
Author information
Authors and Affiliations
Additional information
This work was supported by Grant HL-17535 from the National Institutes of Health.
Rights and permissions
About this article
Cite this article
Yoshida, A., Wessels, M. Origin of the multiple components of human α1-antitrypsin. Biochem Genet 16, 641–649 (1978). https://doi.org/10.1007/BF00484720
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF00484720