Abstract
Hemoglobin (Hb) is a protein and its functional form has a tetrameric structure. This structure is the result of a combination of four sub-units called globin and indicates the dynamic interaction between them. Each subunit has a ring-shaped organic molecule called a heme that contains an iron atom; Heme is a group that mediates the reversible binding of oxygen by hemoglobin. This research was performed to observe the image of Hb by an atomic force microscope (AFM) and measure the physical function of athletes. For this purpose, based on the principle of AFM imaging, the hemoglobin crosslinking method was used to measure the morphology and size of cross-linked Hb, glutaraldehyde and Hb diameter were detected to prepare cross-linked Hb samples with different molar ratio, the activity of peroxidase was detected by Trinder reaction. The AFM was used to detect the influence of physiological environment changes such as pH, temperature, oxygen partial pressure and osmotic pressure on the absorption spectrum of Hb imaging. Results showed that the size of the uncrosslinked Hb was 6.64 nm. With the increase of the molar ratio of glutaraldehyde to Hb, the number of Hb molecules involved in the crosslinking increased, and the molecular size increased. During the crosslinking process, the aggregation of the cross-linked molecules would make the particle size of some Hb molecules reach 80-100 nm. The peak height, peak position and peak shape of the characteristic absorption peaks of pH to hemoglobin at 550 and 589 nm occurred. When the temperature changes continuously in the range of 30-55℃, the peak height of Hb absorption spectrum of normal red blood cells at 550 nm and 589 nm decreases gradually with the increase of temperature, and the peak shape at 610 nm changes obviously at 42℃, which indicates that the molecular structure of Hb changes; the absorption spectrum curve of deoxygenation disappears at 500 nm, the oxygen-binding capacity of Hb is very low, and the oxygen affinity and oxygenated hemoglobin are low (The concentration of HbO2) decreased, the osmotic pressure increased, the RBC dehydrated, the volume decreased, and the concentration of Hb increased. Conclusion: It is more accurate and comprehensive to use AFM to observe athletes' hemoglobin.
Highlights
The physiological advantage of the presence of hemoglobin (Hb) in red blood cells is the improvement in oxygen delivery to tissues and organs
Morphology and size of cross-linked hemoglobin Atomic force microscopy showed that the molecular size of uncross-linked hemoglobin was about 6.64 nm (Figure 2-1), which was similar to the result of X-ray diffraction; it was the image with the molar ratio of glutaraldehyde to the hemoglobin of 1:1, and the particle size of uncross-linked hemoglobin was similar to that of uncross-linked hemoglobin, and the number of molecules with intermolecular cross-linking was less
When the molar ratio is 2:1, the particle size of cross-linked Hb is mostly kept at 20-30 nm; when the molar ratio is 10:1, the particle size below 30 nm accounts for the majority; when the molar ratio is 20:1, the cross-linked molecule diameter is about 30 nm; with the increase of the molar ratio, the cross-linked hemoglobin molecular size changes little, but the number of crosslinked molecules increases; the agglomeration of crosslinked molecules will make the particle size of some Hb molecules increase during the crosslinking process up to 80-100 nm
Summary
The physiological advantage of the presence of hemoglobin (Hb) in red blood cells is the improvement in oxygen delivery to tissues and organs. The imaging of athletes' body functional hemoglobin is observed by atomic force microscope, which overcomes the traditional micro-spectrophotometric system's long detection time due to the single-channel optical detection, which is difficult to carry out the spectral detection of time resolution requirements and multi-component material analysis [5, 6]. In addition to the optical density measurement, spectral absorption measurement and fluorescence measurement of biological tissues, cells, cell products, bacteria and parasites, the dynamic study of the changes of the molecules in a single living cell with physiological and biochemical conditions can be carried out [7], the detection of apoptosis process, the monitoring of cell discharge (secretion) during the opening and closing of cell ion channels, and the monitoring of single living cells with multi-molecular probes Cell fluorescence detection and spectral analysis of micro rapid biological events [8,9,10,11]
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