期刊
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
卷 1804, 期 6, 页码 1376-1384出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2010.02.014
关键词
Carbonic anhydrase XII; Quantum dot; Dansylamide; Polylysine
资金
- National Institutes of Health (NIH) [CA113746, CA132034]
- National Science Foundation (NSF) [DMR-0705767, EPS-0814442]
- UTA
- NSF and DHS [2008-DN-077-ARI016-03]
- U.S. Army Medical Research Acquisition Activity (USAMRAA) [W81XWH-05-C-0101, BC095348]
- EPSCoR
- Office Of The Director [0814442] Funding Source: National Science Foundation
Due to prevalence of negative charges on the protein surface, opposite to the active site pocket of human carbonic anhydrase XII (hCA XII), both positively charged CdTe quantum dots (Qds(+)) and polylysine electrostatically interact with the enzyme, and such interaction does not influence the catalytic activity of the enzyme. However, both these cationic macromolecules differently modulate the active site environment of the enzyme. The steady-state kinetic data revealed that whereas polylysine exhibited no influence on dansylamide (DNSA) dependent inhibition of the enzyme, Qds(+) overcame such an inhibitory effect, leading to almost 70% restoration of the catalytic activity of the enzyme. We provide evidence that DNSA remains bound to the enzyme upon interaction with both polylysine and Qds(+). Arguments are presented that the above differential feature of polylysine and Qds(+) on hCA XII is encoded in the rigidity versus flexibility of these cationic macromolecules. (C) 2010 Elsevier B.V. All rights reserved.
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