Protein and Proteomics Research Group, Department of Biochemistry, Faculty of Science, Khon Kaen University, Khon Kaen 40002, Thailand.
Protein J. 2012 Aug;31(6):466-76. doi: 10.1007/s10930-012-9424-7.
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.
暹罗鳄的血红蛋白、α-链、β-链和碎片化血红蛋白均表现出抗菌和抗氧化活性。血红蛋白的抗菌和抗氧化特性不依赖于血红素结构，而可能源于其一级结构中存在的氨基酸残基和结构组成。此外，通过反相高效液相色谱（RP-HPLC）分析得到了 13 个纯化的活性肽，这些活性肽对应于α-球蛋白链和β-球蛋白链的片段，主要位于 N 端和 C 端部分。这些活性肽作用于细菌细胞膜。暹罗鳄的球蛋白链与尼罗鳄的序列具有相似的氨基酸。α-链和β-链的新氨基酸取代与血红素结合位点或碳酸氢根离子结合位点无关，但通过与细菌膜的相互作用可能很重要。
