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CAS No 9031-37-2 , 2-amino-3,5-diazabicyclo[3.1.0]hex-2-en-4-one

  • Name: 2-amino-3,5-diazabicyclo[3.1.0]hex-2-en-4-one
  • Synonyms: MLS002702958; Amplimexon; 59643-91-3; 4-Imino-1,3-diazabicyclo(3.1.0)hexan-2-one;2-amino-3,5-diazabicyclo[3.1.0]hex-2-en-4-one;Imexon; Imexonum [INN-Latin];
  • CAS Registry Number:
  • Safety Statements:
    Hazard Codes B
    WGK Germany 3
  • Hazard Symbols: B
  • EINECS: 232-868-3
  • Molecular Weight: 111.102
  • InchiKey: BIXBBIPTYBJTRY-UHFFFAOYSA-N
  • InChI: InChI=1S/C4H5N3O/c5-3-2-1-7(2)4(8)6-3/h2H,1H2,(H2,5,6,8)
  • Molecular Formula: C4H5N3O
  • Molecular Structure:CAS No:9031-37-2 2-amino-3,5-diazabicyclo[3.1.0]hex-2-en-4-one

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References of 2-amino-3,5-diazabicyclo[3.1.0]hex-2-en-4-one
Title: Ceruloplasmin
CAS Registry Number: 9031-37-2
Synonyms: Caeruloplasmin; ferroxidase
Literature References: Intensely blue colored copper-containing glycoprotein of the a2-globulin fraction of mammalian blood; it is the principal copper transport protein and is believed to play an important role in iron mobilization via its ferroxidase activity. First reported by C. G. Holmberg, Acta Physiol. Scand. 8, 227 (1944). Isoln, purification and description of properties of porcine and human ceruloplasmin: C. G. Holmberg, C. B. Laurell, Acta Chem. Scand. 2, 550 (1948). Ceruloplasmin accounts for 90-95% of the circulating copper in normal mammals. Its concentration increases by a factor of 2 to 3 during pregnancy and varies significantly in several diseases and hormonal conditions. Prepd by Cohn cold ethanol fractionation: Cohn et al., J. Am. Chem. Soc. 68, 459 (1946); Steinbuch, Quentin, Nature 183, 323 (1959); and further purified from fraction IV: Sanders et al., Arch. Biochem. Biophys. 84, 60 (1959); US 3003918 (1961 to Merck & Co.). Different mol wts have been reported for human ceruloplasmin, ranging from 126,000 to 160,000; the most generally accepted is 134,000 ±3000, cf. L. Ryder, I. Bj?rk, Biochemistry 15, 3411 (1976). Chemical and structural studies of porcine ceruloplasmin: Osaki et al., J. Biochem. (Tokyo) 48, 190 (1960); 50, 24, 29 (1961); Mukasa et al., Biochim. Biophys. Acta 168, 132 (1968); Matsunaga, Nosoh, ibid. 215, 280 (1970); of human: Kasper, Deutsch, J. Biol. Chem. 238, 2325 (1963); Jamieson, ibid. 240, 2019 (1965); Poillon, Bearn, Biochim. Biophys. Acta 127, 407 (1966); Simons, Bearn, ibid. 175, 260 (1969); Ryden, Eur. J. Biochem. 26, 380 (1972); T. G. Samsonidze et al., Int. J. Pept. Protein Res. 14, 161 (1979); V. N. Zaitsev et al., Kristallografiya 25, 174 (1980), C.A. 92, 210415q (1980). Human metabolism: Kekki et al., Nature 209, 1252 (1966). Reviews of biological role: E. Frieden, H. S. Hsieh, Adv. Exp. Med. Biol. 74, 505-529 (1976); J. M. C. Gutteridge, Ann. Clin. Biochem. 15, 293-296 (1978). Comprehensive review: S. H. Laurie, E. S. Mohammed, Coord. Chem. Rev. 33, 279-312 (1980).
Properties: Absorption max: 280, 610 nm (E1%1cm 14.9, 0.68). Electrophoretic mobility (cm/volt/sec): -5.05 ′ 10-5 at pH 7.0 (0.1M phosphate buffer); -5.32 ′ 10-5 at pH 8.6 (0.1M barbital sodium buffer).
Absorption maximum: Absorption max: 280, 610 nm (E1%1cm 14.9, 0.68)