Erratum to: A smallest 6 kda metalloprotease, mini-matrilysin, in living world: a revolutionary conserved zinc-dependent proteolytic domain- helix-loop-helix catalytic zinc binding domain (ZBD)

  • Wei-Hsuan Yu1Email author,

    Affiliated with

    • Po-Tsang Huang1, 2,

      Affiliated with

      • Kuo-Long Lou1, 2, 3, 4,

        Affiliated with

        • Shuan-Su C Yu1 and

          Affiliated with

          • Chen Lin1

            Affiliated with

            Journal of Biomedical Science201219:87

            DOI: 10.1186/1423-0127-19-87

            Received: 17 September 2012

            Accepted: 24 September 2012

            Published: 6 October 2012

            The original article was published in Journal of Biomedical Science 2012 19:54

            There is a major mistake in the order of Figure 5 to Figure 7 in[1]. We replce the Figure 5 and Figure 6 in[1] with new corrected Figures of Figure1 and Figure2. We also replace the correct original order of Figure 6 and Figure 7 in[1] with Figure2 and Figure3 in this correction. Sorry for the inconveniences!
            Figure 1

            Combination of 0.05% Triton and 0.2 mg/ml heparin give the optimal refolding activities to cleave the synthetic coumarin-labelled peptide substrate, Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2. Panel A: Shows the refolded ZBD activities increased in dose-dependent manner. In the absence of the refolding accessory factors, Triton X-100 and heparin. The significant reduced activities in the high-concentration (> 100 μg/ml) was observed which could be due to autolysis. Panel B: Under 37°C incubation for 18 hours, Triton X-100 and heparin can prevent the activity loss. (All experiments were repeated at two batch of purification and refolding preparation and data collected from a representative experiments)

            Figure 2

            The polymerization of the 6 kDa ZBD of MMP-7 in pentomer and Octmer demonstrate the significant proteolytic activities towards to the CM-transferrin substrate in CM-transferrin zymographic assay. 300 μg of craboxylmethylated transferrin (CM-transferrin) was co-polymerized with SDS-PAGE as a substrate gel for analyzing the MMP-7 activities in situ

            Figure 3

            Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 assay for characterization of refolded ZBD. Panel A: Under the optimized conditions, the refolded ZBD shows increasing enzymatic activity in dose-dependent manner. No significant activity loss was found in the high concentration situation. Panel B: approximately 6 ng/ml refolded ZBD shows the increasing activity during the time course study and no significant activity loss during overnight incubation. Panel C: Recombinant ZBD can be inhibited by 10 nM EDTA, 1 mM CoCl2 and synthetic inhibitors, 50 nM BB94 & SC44463 and CoCl2, but not b6 250 nM Phosphoramidon. (All experiments were repeated at two batch of purification and refolding preparation and data collected from a representative experiments)


            Authors’ Affiliations

            Institute of Biochemistry and Molecular Biology, National Taiwan University, College of Medicine
            Graduate Institute of Oral Biology, National Taiwan University, College of Medicine
            NTU-DRCP Lectures and Core for Membrane Proteins, Center for Biotechnology, National Taiwan University
            Institute of Biotechnology, National Taiwan University


            1. Yu WH, Huang PT, Lou KL, Yu SS, Lin C: A Smallest 6 kDa Metalloprotease, Mini-matrilysin, in Living World: a Revolutionary Conserved Zinc-Dependent Proteolytic Domain- Helix-Loop-Helix Catalytic Zinc Binding Domain (ZBD). J Biomed Sci. 2012, 19: 54-10.1186/1423-0127-19-54.PubMed CentralView ArticlePubMed


            © Yu et al.; licensee BioMed Central Ltd. 2012

            This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://​creativecommons.​org/​licenses/​by/​2.​0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.