Smales, C. Mark and Blackwell, Leonard F. (2003) Lysozyme conjugate immune complex formation and the effects on substrate hydrolysis. Biochemical and Biophysical Research Communications, 304 (4). pp. 818-824. ISSN 0006-291X. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)
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The defined estrone glucuronide-lysozyme conjugate E3, that is acylated solely at K33, was used as a probe for the steric requirements of the active site cleft of chicken type lysozymes. When the immune complex was formed with an anti-estrone glucuronide antiserum, the rate of lysis of the E3 conjugate with the large bacterial substrate Micrococcus lysodeikticus was inhibited by over 90%. However, when the small hexamer of N-acetyl glucosamine was used as the substrate, the rate of hydrolysis by the immune complex was accelerated by 350% compared with the control rate. Thus, inhibition by the anti-estrone glucuronide cannot be caused simply by steric occlusion of the active site. Other factor(s) in the immune complex activate the hydrolysis reaction, most likely by favouring the conformations that lead to the transition state. (C) 2003 Elsevier Science (USA). All rights reserved.
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||Mark Smales|
|Date Deposited:||09 Sep 2008 05:07|
|Last Modified:||09 Jun 2014 08:37|
|Resource URI:||https://kar.kent.ac.uk/id/eprint/6215 (The current URI for this page, for reference purposes)|