Mechanism of the Effect of Lactate on the Structure of Myoglobin in the in Vitro Hatching Model

In order to study the interaction mechanism between lactate and myoglobin(Mb)heme prosthetic group,the longissimus dorsi was used as the raw material. Mb was separated and purified before adding calcium lactate. It was stored at 4 ℃ for 0,12,24,36,and 72 h,using ultraviolet-visible absorption spectrum,fluorescence spectrum and circular dichroism spectrum to determine the absorbance of the characteristic peak. The results showed that the absorption intensity of the ultraviolet-visible spectrum at the characteristic peak of 409 nm at four time points during refrigeration was slightly increased,but the peak position and peak shape barely changed;the intensity of the emission peak of the fluorescence spectrum at 597 nm weakened. The position of the emission peak of the porphyrin ring of Mb did not shift,but the fluorescence intensity weakened with the extension of storage time;circular dichroism chromatography showed that the shape and shoulder of the three characteristic peaks in the far ultraviolet region of 192,208 and 222 nm in the control and treatment groups The position of the peak did not change significantly,and the pattern at 190~240 nm in the calcium lactate treatment group was smooth like the control group. It shows that the covalent addition of lactate and Mb does not occur on the heme prosthetic group,but regulates myoglobin through non-heme ligand binding.