title: Comparison of recombinant α-hemoglobin from Crocodylus siamensis expressed in different cloning vectors and their biological properties.
abstract: Hemoglobin (Hb) is an important component in red blood cells of the vertebrate. It is a major respiratory protein with oxygen or carbon dioxide transport function. Hb has been reported to contain bioactive peptides which have antibacterial and antioxidant activities. In this study, the alpha-chain hemoglobin(αHb) gene of Crocodylus siamensis was cloned into the three different expression vectors and expressed in Escherichia coli BL21 (DE3). The recombinant αHb proteins from all constructs could be expressed and purified. The result from UV-visible absorption spectra showed a similar pattern of all recombinant proteins to the oxy-hemoglobin form of intact Hb. The different recombinant αHb could exhibit antioxidant activities. All recombinant proteins could inhibit the growth of Bacillus spp. Especially, most of the recombinant proteins could inhibit the growth of Bacillus amyloliquefaciens TISTR 1045 better than intact one. The result obtained from this study can provide us further information about the possibility using of αHb as a supplementary food.
authors.affiliation: Department of Biochemistry, Faculty of Science, Khon Kaen University, Khon Kaen, 40002, Thailand; Protein and Proteomics Research Center for Commercial and Industrial Purposes (ProCCI), Khon Kaen University, Khon Kaen, 40002, Thailand.
authors.forename: Surachai
authors.initials: S
authors.lastname: Maijaroen
authors.affiliation: Department of Biochemistry, Faculty of Science, Khon Kaen University, Khon Kaen, 40002, Thailand; Protein and Proteomics Research Center for Commercial and Industrial Purposes (ProCCI), Khon Kaen University, Khon Kaen, 40002, Thailand.
authors.forename: Preeyanan
authors.initials: P
authors.lastname: Anwised
authors.affiliation: Department of Biochemistry, Faculty of Science, Khon Kaen University, Khon Kaen, 40002, Thailand; Protein and Proteomics Research Center for Commercial and Industrial Purposes (ProCCI), Khon Kaen University, Khon Kaen, 40002, Thailand.
authors.forename: Sompong
authors.initials: S
authors.lastname: Klaynongsruang
authors.affiliation: Division of Pharmacognosy and Toxicology, Faculty of Pharmaceutical Sciences, Khon Kaen University, Khon Kaen 40002, Thailand; Protein and Proteomics Research Center for Commercial and Industrial Purposes (ProCCI), Khon Kaen University, Khon Kaen, 40002, Thailand.
authors.forename: Sakda
authors.initials: S
authors.lastname: Daduang
authors.affiliation: Department of Microbiology, Faculty of Science, Khon Kaen University, Khon Kaen, 40002, Thailand; Protein and Proteomics Research Center for Commercial and Industrial Purposes (ProCCI), Khon Kaen University, Khon Kaen, 40002, Thailand. Electronic address: atcha@kku.ac.th.
authors.forename: Atcha
authors.initials: A
authors.lastname: Boonmee
mesh_terms: D000489:Alligators and Crocodiles / Q000235:genetics*; D020816:Amino Acid Motifs; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology; D001407:Bacillus / Q000187:drug effects / Q000254:growth & development; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D005822:Genetic Vectors / Q000235:genetics* / Q000378:metabolism; D006454:Hemoglobins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism / Q000494:pharmacology*; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism / Q000494:pharmacology*; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology
chemical_list: D000900:Anti-Bacterial Agents; D006454:Hemoglobins; D010446:Peptide Fragments; D011994:Recombinant Proteins; C070077:alpha(A) globin
keywords: Alpha hemoglobin; Crocodylus siamensis; Protein expression; Protein purification; Recombinant protein