Smales, C. Mark and Moore, Christopher H. and Blackwell, Leonard F. (1999) Characterization of lysozyme-estrone glucuronide conjugates. The effect of the coupling reagent on the substitution level and sites of acylation. Bioconjugate Chemistry, 10 (4). pp. 693-700. ISSN 1043-1802. (doi:10.1021/bc9900441) (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)
Estrone glucuronide conjugates of hen egg white lysozyme were prepared by the mixed anhydride and active ester coupling procedures. Both methods gave good yields of conjugates, but the active ester procedure gave a more diverse range of products, making it less suitable for preparing conjugates for homogeneous enzyme immunoassay. Conjugation of lysozyme with estrone glucuronide by the mixed anhydride procedure gave one major derivative exclusively acylated at lysine residue 33 whereas conjugation by the active ester method gave six derivatives which were acylated at one or more of lysine residues 33, 97, and 116. None of the lysine residues 1, 13, and 96, or the N-terminal a-amino group, were acylated in any of the conjugates isolated. The correlation of the conjugate structures with the protein environments of the amino groups in the crystal structure of lysozyme suggested that the sites of acylation were determined not only by the chemical nature of the acylating reagent but also by the surface accessibility and nucleophilicity of the individual lysine residues.
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||Mark Smales|
|Date Deposited:||14 Jun 2009 09:50|
|Last Modified:||22 Apr 2014 14:24|
|Resource URI:||https://kar.kent.ac.uk/id/eprint/6205 (The current URI for this page, for reference purposes)|