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The Primary Structure of beta super(I)-Chain of Hemoglobin from Snake Sindhi Krait (Bungarus sindanus sindanus)
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The Primary Structure of beta super(I)-Chain of Hemoglobin from Snake Sindhi Krait (Bungarus sindanus sindanus)
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The Primary Structure of beta super(I)-Chain of Hemoglobin from Snake Sindhi Krait (Bungarus sindanus sindanus)
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Journal Article
The Primary Structure of beta super(I)-Chain of Hemoglobin from Snake Sindhi Krait (Bungarus sindanus sindanus)
2016
Overview
The amino acid sequence of beta super(I)-globin chain from Sindhi Krait (Bungarus sindanus sindanus) was determined to study the molecular evolution among snakes. The hemoglobin was isolated from the red blood cells and was analyzed by ion-exchange chromatography (IEX). The crude globin was subjected to reversed phased-high performance liquid chromatography (RP-HPLC) using C4 column. The N-terminal sequences of intact globin chains and tryptic peptides were determined by Edman degradation in a pulsed liquid gas phase sequencer using an online Phenylthiohydantoin analyzer. Sindhi Krait is expected to express three hemoglobin components that are composed of beta super(II), beta super(I), alpha super(D) and alpha super(A)-globin chains, as apparent by IEX, RP-HPLC and N-terminal sequence analyses. Sequence alignment and phylogenetic analyses of beta super(I) globin chain from Sindhi Krait showed closest relationship with beta super(I) globin chain from Rattlesnake, Water snake and Indigo snake. Interestingly, comparison of primary sequence of beta super(I) globin chain of Sindhi Krait with human beta chain revealed 63 % similarity along with the retention of all heme contact points. Variations among the two sequences were prominent at alpha beta contact points and in regions directly not important for function.
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