Smalley, John W, Birss, Andrew J, Szmigielski, Borys and Potempa, Jan
(2008)
Mechanism of methaemoglobin breakdown by the lysine-specific gingipain of the periodontal pathogen Porphyromonas gingivalis.
Biological chemistry, 389 (9).
pp. 1235-1238.
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Abstract
Abstract The R- and K-gingipain proteases of Porphyromonas gingivalis are involved in proteolysis of haemoglobin from which the defensive dimeric haem pigment is formed. Whilst oxyhaemoglobin is refractory towards K-gingipain, methaemoglobin is rapidly degraded. Ligation of methaemoglobin with N3-, which effectively blocks haem dissociation from the protein, prevented haemoglobin breakdown. Haem-free globin was rapidly degraded by K-gingipain. These data emphasise the need for haemoglobin oxidation which encourages haem dissociation and makes the haem-free globin susceptible to proteolytic attack.
Item Type: | Article |
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Additional Information: | published online: 17/09/2008. Citation Information. Biological Chemistry. Volume 389, Issue 9, Pages 1235–1238, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2008.140, September 2008 |
Uncontrolled Keywords: | Animals, Horses, Porphyromonas gingivalis, Cysteine Endopeptidases, Adhesins, Bacterial, Methemoglobin, Ligands, Gingipain Cysteine Endopeptidases |
Subjects: | ?? RK ?? |
Divisions: | Faculty of Health and Life Sciences > Institute of Life Courses and Medical Sciences > School of Dentistry |
Depositing User: | Symplectic Admin |
Date Deposited: | 05 Dec 2008 10:17 |
Last Modified: | 15 Mar 2024 06:52 |
DOI: | 10.1515/bc.2008.140 |
Publisher's Statement : | The Version of Record (VoR) is available at www.biochemj.org |
Related URLs: | |
URI: | https://livrepository.liverpool.ac.uk/id/eprint/946 |