Dave, Sandeep and Mahajan, Sahil and Chandra, Vemika and Dkhar, H Kitdorlang and Sambhavi, - and Gupta, Pawan (2010) Specific molten globule conformation of stem bromelain at alkaline pH. Archives of biochemistry and biophysics, 499 (1-2). pp. 26-31. ISSN 1096-0384
Full text not available from this repository. (Request a copy)Abstract
Stem bromelain (SBM), a therapeutic protein, is rapidly absorbed across the gut epithelium. Because SBM encounters an alkaline pH at its principal site of absorption, we investigated the alkaline-induced denaturation of SBM. From pH 7 to 10, the protein's secondary structure remained the same, although a slight loss of tertiary structure was observed. Above pH 10, there was a significant and irreversible loss of secondary and tertiary structure. At pH 10, SBM showed enhanced tryptophan fluorescence, however, the number of accessible tryptophans remained the same. The thermodynamics of temperature transition at pH 7 and 10 were strikingly different, with the former showing a two-phase transition endotherm, and the latter a broad non-two-state transition. At pH 10, SBM showed a significant increase in 8-anilino-1-naphthalene-sulfonate binding relative to the native state, suggestive of a specific molten globule (SMG) state. These studies suggest a distinct conformational rearrangement in SBM, at the protein's isoelectric point.
| Item Type: | Article |
|---|---|
| Additional Information: | Copyright of this article belongs to Elsevier Science |
| Uncontrolled Keywords: | Protein folding; Alkaline denaturation; Bromelain; Molten globule; Temperature endotherm; Thermodynamics |
| Subjects: | Q Science > QR Microbiology |
| Depositing User: | Dr. K.P.S.Sengar |
| Date Deposited: | 08 Dec 2011 19:18 |
| Last Modified: | 08 Dec 2011 19:18 |
| URI: | http://crdd.osdd.net/open/id/eprint/515 |
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