ArticleThe protein journal2012
Complete amino acid sequence of globin chains and biological activity of fragmented crocodile hemoglobin (Crocodylus siamensis).
Article in The protein journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 33 citations in OpenAlex.
- Protective Effect of Crocodile Hemoglobin and Whole Blood Against Hydrogen Peroxide-Induced Oxidative Damage in Human Lung Fibroblasts (MRC-5) and Inflammation in Mice.Inflammation · 2017Article
- Immunological properties of oxygen-transport proteins: hemoglobin, hemocyanin and hemerythrin.Cellular and molecular life sciences : CMLS · 2017Review
- Antimicrobial activity and safety evaluation of peptides isolated from the hemoglobin of chickens.BMC microbiology · 2016Article
- Cloning, Expression, and Characterization of Siamese Crocodile (Crocodylus siamensis) Hemoglobin from Escherichia coli and Pichia pastoris.The protein journal · 2016Article
- Full-Length cDNA, Prokaryotic Expression, and Antimicrobial Activity of UuHb-F-I from Urechis unicinctus.BioMed research international · 2016Article
- An investigation of antioxidant and anti-inflammatory activities from blood components of Crocodile (Crocodylus siamensis).The protein journal · 2014Article
- Purification, characterization, and crystallization of Crocodylus siamensis hemoglobin.The protein journal · 2014Article
- Antimicrobial peptides in reptiles.Pharmaceuticals (Basel, Switzerland) · 2014Article
- Purification and characterization of antioxidant peptides from leukocyte extract of Crocodylus siamensis.The protein journal · 2014Article
- Molecular cloning and expression of α-globin and β-globin genes from crocodile (Crocodylus siamensis).The protein journal · 2013Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hemoglobin, α-chain, β-chain and fragmented hemoglobin of Crocodylus siamensis demonstrated both antibacterial and antioxidant activities. Antibacterial and antioxidant properties of the hemoglobin did not depend on the heme structure but could result from the compositions of amino acid residues and structures present in their primary structure. Furthermore, thirteen purified active peptides were obtained by RP-HPLC analyses, corresponding to fragments in the α-globin chain and the β-globin chain which are mostly located at the N-terminal and C-terminal parts. These active peptides operate on the bacterial cell membrane. The globin chains of Crocodylus siamensis showed similar amino acids to the sequences of Crocodylus niloticus. The novel amino acid substitutions of α-chain and β-chain are not associated with the heme binding site or the bicarbonate ion binding site, but could be important through their interactions with membranes of bacteria.
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Registered trials
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