N�89 and C�274 Truncated Enzymes of Chondroitinase ABC I Regain More Imperturbable Microenvironments Around Structural Components in Comparison to their Wild Type

Omidi-Ardali, H. and Aminian, M. and Golestani, A. and Shahaboddin, M.E. and Maleki, M. (2019) N�89 and C�274 Truncated Enzymes of Chondroitinase ABC I Regain More Imperturbable Microenvironments Around Structural Components in Comparison to their Wild Type. Protein Journal.

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Abstract

Immune response stimulation and inactivation of chondroitinase ABC I in physiological condition have been limited its use in various clinical conditions as a bacterial enzyme drug. In the present study, we have investigated some structural and functional features of N�89, C�274 and N�89C�274; three designed truncated cABC I, in order to clarify the unclear role of two terminal parts of cABC I i.e., the 1�89 and 747�1021 amino acids sequences of the full length enzyme through truncation. As a result, the numbers of potential epitopes, the susceptibility to trypsin digestion, ANS fluorescence spectra, and fluorescence quenching using KI and acrylamide were diminished for N�89 and C�274 in comparison to the wild type. Secondary and tertiary structure investigation for N�89 and C�274 revealed that the intrinsic fluorescence was increased and Far-UV CD spectra were changed accordingly. Relative to the wild type enzyme, 0.164, 0.195 remaining activity and lack of activity was shown with the zymographic assay for N�89, C�274 and N�89C�274 variants, respectively. The diminished enzyme activity and structural changes suggested a reorientation of microenvironments interactions including cation�� interactions around structural elements toward lowering regional mobility. Constructing applicable truncated cABC I with improved features could be regarded as a strategy to regain new possible functional advantages over the full length enzyme. © 2019, Springer Science+Business Media, LLC, part of Springer Nature.

Item Type: Article
Additional Information: cited By 0
Subjects: Nutrition
Biochemistry, Genetics and Molecular Biology
Divisions: Faculty of Medicine > Basic Sciences > Department of Biochemistry
Depositing User: ART . editor
Date Deposited: 07 May 2019 11:30
Last Modified: 07 May 2019 11:30
URI: http://eprints.kaums.ac.ir/id/eprint/3748

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