Chemical modification of glucose oxidase: possible formation of molten globule-like intermediate structure.

Abstract:

:Chemical modification of lysine residues in glucose oxidase was carried out using citraconic anhydride. Modification brought about changes in the kinetic properties of the enzyme as evident by substantial lowering of V(max) and K(m). Enhancement of tryptophan fluorescence was observed with a dramatic change in its pH dependence due to modification. Near- and far-UV circular dichroism spectra of the native and modified forms suggested formation of molten globule-like structures, further supported by 8-anilino-1-naphthalenesulfonic acid fluorescence which indicated higher exposure of hydrophobic residues as a result of chemical modification.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Hosseinkhani S,Ranjbar B,Naderi-Manesh H,Nemat-Gorgani M

doi

10.1016/S0014-5793(04)00134-6

keywords:

subject

Has Abstract

pub_date

2004-03-12 00:00:00

pages

213-6

issue

1-3

eissn

0014-5793

issn

1873-3468

pii

S0014579304001346

journal_volume

561

pub_type

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