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High‐level expression and characterization of a glycosylated human cementum protein 1 with lectin activity
Author(s) -
RomoArévalo Enrique,
Arzate Higinio,
MontoyaAyala Gonzalo,
RodríguezRomero Adela
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12032
Subject(s) - circular dichroism , lectin , chemistry , random coil , biochemistry , pichia pastoris , random hexamer , glycosylation , molecular mass , biomineralization , microbiology and biotechnology , biology , enzyme , recombinant dna , paleontology , gene
This work aims to contribute to the knowledge of human cementum protein 1 (CEMP1), its conformational characteristics and influence during the biomineralization process. The results revealed that hrCEMP1 expressed in Pichia pastoris is a 2.4% glycosylated, thermostable protein which possesses a molecular mass of 28 770 Da. The circular dichroism spectrum indicated a secondary structure content of 28.6% of alpha‐helix, 9.9% of beta‐sheet and 61.5% of random‐coil forms. Biological activity assays demonstrated that hrCEMP1 nucleates and regulates hydroxyapatite crystal growth. Hereby, it is demonstrated for the first time that CEMP1 has a (C‐type) lectin‐like activity and specifically recognizes mannopyranoside. The information produced by this biochemical and structural characterization may contribute to understand more fully the biological functions of CEMP1.