Study On Determination Of Albumin In Animal Body Fluid By Spectrographic Methods

In recent years, along with our country animal husbandry's unceasing development, the poultry variety and quantity had great scope increase. Corresponding, our country's livestock and poultry diseases and the type of frequency also greatly to increase, significantly, this has created the huge economic loss for our country's poultry industry. Therefore, the rapid diagnosis of animal diseases is very important research subject.The serum albumin is the content richest protein in the blood, which in animal body fluids in the content of a certain extent, can be used as the basis for the diagnosis of the disease. Using the new research discovery's spectrum probe examination protein's content, and applied animal protein in the body fluids or the determination of biological products in the determination of protein, is a very meaningful work..This article focuses on small organic molecules diphenylamine sulfonic acid sodium, the XO and naphthol Green B and protein interactions, applied research and animal body fluids in the determination of protein.Its paper primary coverage is as follows:The results and methods for study of reaction mechanism between small organic molecules with protein were reviewed with 84 references.The xylenol orange and the Cu(II) complex probe to determine the protein content have been studied. The Resonance light scattering spectrum of the characteristics of the XO and Cu (II) complex with bovine serum albumin have been studied. This method was applied to the determination of bovine urine and compared to Bradford method with satisfactory results.The diphenylamine sulfonic acid sodium probe to determine the protein content have been studied by resonance scattering spectrum (RLS). The diphenylamine sulfonic acid sodium with bovine serum albumin resonance scattering spectrum of the characteristics have been studied. This method was applied to the determination of bovine urine and compared to Bradford method with satisfactory results.The binding characteristics of Naphthol green B(NGB) with bovine serum albumin(BSA) have been studied by spectroscopy method in aqueous solution. It is proved that static quenching exits between NGB-BSA super-molecular complex. The formation constant KA and the thermodynamic functions (such asâ–³G,â–³H andâ–³S) for the reaction have all been measured; temperatures on the formation constant of Naphthol green B with BSA was also studied; According to the thermodynamic parameters, the hydrogen bonding and van'der Waals forces played major role in the interaction. The effect of Naphthol green B on the conformation of BSA has also been analyzed using synchronous fluorescence spectroscopy; The binding distance between Naphthol green B and BSA and the transfer efficiency have been obtained based on the mechanism of Forster energy transfer.Studies discovered: In the high temperature acid solution, naphthol green B has the discoloration response; BSA's accession to the naphthol Green B inhibition reaction to the fading effect, which further define naphthol Green B and bovine serum albumin can bind.