References
- Parisi A F, Vallee B L. Isolation of a zinc α2M from human serum. Biochemistry 1970; 9: 2421–6
- Barrett A J, Starkey P M. The interaction of α2M with proteinases. Characteristics and specificity of the reaction and a hypothesis concerning its molecular mechanism. Biochem J 1973; 133: 709–24
- Laurell C B, Jeppson J-O. Protease inhibitors in plasma. The Plasma Proteins, Function and the Genetic Control. 2nd edition, F WP Putman. Academic Press, New York 1975; Vol. 1: 229–264
- Koj A. Comparison of the synthesis and secretion of plasma albumin, fibrinogen and a α2-macroglobulin by slices of Morris hepatomas and rat liver. Br J Exp Path 1980; 61: 332–38
- Gliemann J, Larsen T R, Sottrup-Jensen L. Cell association and degradation of α2Macroglobulin-Trypsin complexes in hepatocytes and adipocytes. Biochim Biophys Acta 1983; 756: 230–37
- Hovi T, Mosher D F, Vaheri A. Cultured human monocytes synthesize and secrete α2-macroglobulin. J Exp Med 1977; 145: 1580–89
- White R, Janoff A, Godfrey H P. Secretion of α2 -macroglobulin by human alveolar macrophages. Lung 1980; 158: 9–14
- Van Leuven F, Cassiman J J, van den Berge H. Uptage and degradation of α2-macroglobulin-protease complexes in human cells in culture. Exp Cell Res 1978; 117: 273–82
- Ohlsson K. Interactions in vitro and in vivo between dog trypsin and dog plasma protease inhibitors. Scand J Clin Lab Invest 1971a; 28: 219–23
- Böm N, Shah I, Totovic V, Karitzky D. Combined α1-antitrypsin and α2-macroglobulin deficiency syndrome. Light microscopic evidence of collagenolytic, lastolytic and myolytic tissue lesions. Path Res Pract 1980; 168: 17–35
- Müllertz S. Role of α2-macroglobulin as an inhibitor of fibronolysis. The Physiological Inhibitors of Coagulation and Fibrinolysis, D Collen, B Wiman, M P Vertraiti. Elsevier/North Holland and Biomedical Press, New York 1979; 243–45
- Harpel P C. α2-plasmin inhibitor and α2-macroglobulin-plasmin complexes in plasma. Quantitation by enzyma-like differential antibody immunosorbant assay. J Clin Invest 1981; 68: 46–55
- Sakamoto W. Immunochemical study of B-glucuronidase inhibitor from porcine sublingual gland. Interaction of B-glucuronidase inhibitor with α2-macroglobulin. Biochem Biophys Acta 1975; 411: 195–201
- Stollar B D, Rezuke W. Separation of antihistone antibodies from non-immune histone precipitating serum proteins, predominantly α2-macroglobulin. Arch Biochem Biophys 1978; 190: 398–404
- James K. α2-macroglobulin and its possible role in immune systems. Trends Bil Sci 1980; 5(2)43–47
- Teodurescu M. Characterization and role in autoimmune diseases of the polyclonal B-cell activator produced by T-cells—the helper factor. Immuno-logical Rev 1981; 55: 156–178
- Goutner A, Simmler M C, Tapon J, Rosenfeld C. Modulation by α2-macroglobulin of human lymphocyte proliferation in responses to mitogens and antigen. Differentiation 1976; 5: 171–173
- Tauris P, Andersen P, Christiansen S E. Plaque-forming cell capacity in the senescent. Immunology Lett 1985; 9: 3–8
- Sottrup-Jensen L, Petersen T E, Magnusson S. A thiol ester in α2-macroglobulin cleaved during proteinase complex formation. FEBS Lett 1980; 121: 275–79
- James K, Johnson G, Fudenberg H H. The quantitative estimation of α2-macroglobulin in normal, pathological and cord sera. Clin Chim Acta 1966; 14: 207–214
- Ganrot P O, Schersten B. Serum α2-macroglobulin concentration and its variation with age and sex. Clin Chim Acta 1967; 15: 113–120
- Barrett A J, Brown M A, Sayers C A. The elec-trophoretically ‘slow’ and ‘fast’ forms of the α2-macroglobulin molecule. Biochem J 1979; 181: 401–418