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Interaction of aminoglycoside antibiotics with surface Asp and Glu residues of phosphatidylinositol-specific phospholipase C

Paper ID Volume ID Publish Year Pages File Format Full-Text
18689 42735 2006 6 PDF Available
Title
Interaction of aminoglycoside antibiotics with surface Asp and Glu residues of phosphatidylinositol-specific phospholipase C
Abstract

The aminoglycoside antibiotics such as neomycin, gentamicin, kanamycin and streptomycin stimulated the purified enzyme phosphatidylinositol-specific phospholipases C from Bacillus thuringiensis at pH 5.5. The involvement of net positive charge of aminoglycoside antibiotics (AA) on phosphatidylinositol-specific phospholipases C activation was probed by modifying the carboxyl group of Asp and Glu present in the enzyme by 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDAC). Intrinsic Trp fluorescence of EDAC modified and unmodified PI-PLC in the presence of AA confirmed the interaction of AA with side chain carboxyl group of aspartic and glutamic acid of the enzyme. Thus, the possible interaction of aminoglycoside antibiotics with phosphatidylinositol-specific phospholipases C is predicted to be mediated through the aspartic and glutamic acid residue(s) of the protein.

Keywords
AA, aminoglycoside antibiotics; AChE, acetylcholinesterase; Asp, aspartic acid; DAG, diacylglycerol; EDAC, 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide; Glu, glutamic acid; GPI, glycophosphatidylinositol; mfAChE, membrane form acetylcholinesterase; sACh
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Interaction of aminoglycoside antibiotics with surface Asp and Glu residues of phosphatidylinositol-specific phospholipase C
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 38, Issue 7, 2 May 2006, Pages 899–904
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us