Plasminogen

Literature References: Mol wt ~90,000. The circulating plasma precursor (zymogen) or inactive form of plasmin, q.v. Prepn from blood plasma: Loomis et al., Arch. Biochem. 12, 1 (1947); Oncley et al., J. Am. Chem. Soc. 71, 541 (1949). Purification: Christensen, Smith, Proc. Soc. Exp. Biol. Med. 74, 840 (1950); Kline, J. Biol. Chem. 204, 949 (1953); Hagan et al., ibid. 235, 1005 (1960); Hagan et al., US 3066079 (1962 to Am. Cyanamid); Derechin et al., Biochem. J. 84, 336 (1962); Mertz, Chan, Can. J. Biochem. Physiol. 41, 1811 (1963); D. G. Deutsch, E. T. Mertz, Science 170, 1095 (1970). Physical properties: Davies, Englert, J. Biol. Chem. 235, 1011 (1960). Converted to plasmin by natural activators such as streptokinase, urokinase, or tissue plasminogen activator, q.q.v., through the cleavage of a single arg-val bond. Mechanism of activation: K. C. Robbins et al., ibid. 242, 2333, 4279 (1967). Native plasminogen is a single chain glycopeptide. Two major molecular forms exist, differing in carbohydrate content and separable by affinity chromatography. Mol wt studies: Barlow et al., ibid. 244, 1138 (1969). Sequence studies: K. C. Robbins et al., ibid. 247, 6757 (1972); F. J. Castellino et al., Biochem. Biophys. Res. Commun. 53, 845 (1973). Carbohydrate comp: M. L. Hayes, F. J. Castellino, J. Biol. Chem. 254, 8768, 8772, 8777 (1979). Amino acid sequence and biochemistry: F. J. Castellino, Semin. Thromb. Hemostasis 10, 18 (1984). Biosynthesis and secretion by cultured hepatocytes: J. F. Bohmfalk, G. M. Fuller, Science 209, 408 (1980). Therapeutic use with streptokinase: I. D. Walker et al., Thromb. Haemostasis 51, 204 (1984). Review of fibrinolytic system: D. Collen, ibid. 43, 77-89 (1980). Reviews: Fibrinolysis, D. L. Kline, K. N. N. Reddy, Eds. (CRC, Boca Raton, 1980) 256 pp; F. J. Castellino, Chem. Rev. 81, 431-446 (1981).