| 词条 | Stem bromelain |
| 释义 |
| Name = Stem bromelain | EC_number = 3.4.22.32 | CAS_number = 37189-34-7 | IUBMB_EC_number = 3/4/22/32 | GO_code = | image = | width = | caption = }} 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. References1. ^{{cite journal | vauthors = Buck M | title = Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins | journal = Q. Rev. Biophys. | volume = 31 | issue = 3 | pages = 297–355 | date = August 1998 | pmid = 10384688 }} 2. ^1 {{cite journal | vauthors = Thomas PD, Dill KA | title = Local and nonlocal interactions in globular proteins and mechanisms of alcohol denaturation | journal = Protein Sci. | volume = 2 | issue = 12 | pages = 2050–65 | date = December 1993 | pmid = 8298455 | pmc = 2142326 | doi = 10.1002/pro.5560021206 }} 3. ^{{cite journal | vauthors = Liu Y, Bolen DW | title = The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes | journal = Biochemistry | volume = 34 | issue = 39 | pages = 12884–91 | date = October 1995 | pmid = 7548045 }} 4. ^{{cite journal | vauthors = Blanco FJ, Jiménez MA, Pineda A, Rico M, Santoro J, Nieto JL | title = NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Evidence of trifluoroethanol induced native-like beta-hairpin formation | journal = Biochemistry | volume = 33 | issue = 19 | pages = 6004–14 | date = May 1994 | pmid = 8180228 }} 5. ^{{cite journal | vauthors = Schönbrunner N, Wey J, Engels J, Georg H, Kiefhaber T | title = Native-like beta-structure in a trifluoroethanol-induced partially folded state of the all-beta-sheet protein tendamistat | journal = J. Mol. Biol. | volume = 260 | issue = 3 | pages = 432–45 | date = July 1996 | pmid = 8757805 | doi = 10.1006/jmbi.1996.0412 }} 6. ^{{cite journal | vauthors = Hirota N, Mizuno K, Goto Y | title = Group additive contributions to the alcohol-induced alpha-helix formation of melittin: implication for the mechanism of the alcohol effects on proteins | journal = J. Mol. Biol. | volume = 275 | issue = 2 | pages = 365–78 | date = January 1998 | pmid = 9466915 | doi = 10.1006/jmbi.1997.1468 }} External links
1 : EC 3.4.22 |
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