Stem bromelain

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Stem bromelain
Identifiers
EC no.3.4.22.32
CAS no.37189-34-7
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Stem bromelain (SBM) (EC 3.4.22.32), a proteolytic enzyme, is a widely accepted phytotherapeutical drug member of the bromelain family of proteolytic enzymes obtained from Ananas comosus.[1] Some of the therapeutic benefits of SBM are reversible inhibition of platelet aggregation, angina pectoris, bronchitis, sinusitis, surgical traumas, thrombophlebitis, pyelonephritis and enhanced absorption of drugs, particularly of antibiotics.[2][3][4] Its anti-metastasis and anti-inflammatory activities are apparently independent of its proteolytic activity.[2] Although poorly understood, the diverse pleiotrophic effects of SBM seem to depend on its ability to traverse the membrane barrier,[5][6] a very unusual property of this protein.

References

  1. ^ Buck M (1998) Trifluoroethanol and colleagues: cosolvents come of age. Quart Rev Biophys 31: 297–355.
  2. ^ a b Thomas PD, Dill KA (1993) Local and nonlocal interactions in global proteins and mechanisms of alcohol denaturation. Protein Sci 2: 2050–2065.
  3. ^ Liu Y, Bolen DW (1995) Peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes, Biochemistry 34: 12884–12891.
  4. ^ Blanco FJ, Jiménez MA, Pineda A, Rico M, Santoro J, Nieto JL (1994) NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Evidence of trifluoroethanol induced native-like β-hairpin formation, Biochemistry 33: 6004–6014.
  5. ^ Schönbrunner N, Wey J, Engels J, Gerog H, Kiefhaber T (1996) Native-like β-structure in a trifluoroethanol-induced partially folded state of the all β-sheet protein tendamistate. J Mol Biol 260: 432–445.
  6. ^ Hirota N, Mizuno K, Goto Y (1998) Group additive contributions to the alcohol-induced α-helix formation of melittin. J Mol Biol 275: 365–378.

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