Preparation and efficacy evaluation of polyclonal antibodies against serum albumin of five species / 中国生物制品学杂志

@#Objective To prepare polyclonal antibodies against the serum albumin of human,cattle,sheep,pig and horse,and evaluate their efficacy in the identification of human serum albumin(HSA). Methods The specific polypeptides of human,cattle,sheep,pig and horse serum albumin were prepared by bioinformatics and polypeptide synthesis method,which were coupled with keyhole limpet hemocyanin(KLH)to prepare the peptide antigen after the purity was identified by high performance liquid chromatography(HPLC). Male New Zealand white rabbits were immunized with polypeptide antigens of five species subcutaneously,with 2 for each kind of antigen. The antiserum was then obtained and purified by Protein A affinity chromatography to prepare the polyclonal antibody. The titers and specificity of the polyclonal antibodies were determined by ELISA and Western blot respectively,and the prepared five species of serum albumin were used to identify HSA products. Results The synthetic peptides of human,cattle,sheep,pig and horse serum albumin had a purity of over 91%,and the corresponding polyclonal antibodies all had the titer of 1∶160 000,which showed specific binding with the corresponding antigens and effectively identified the HSA products. Conclusion The polyclonal antibodies of human cattle,sheep,pig and horse serum albumin prepared in this study have good specificity and the preparation process is simple and rapid,suitable for the mass production,which lays a foundation of the development of HSA rapid identification kit.

Clinical pharmacists promoted rational use of human serum albumin in tumor patients based on evidence-based pharmacy / 药学实践杂志

Objective To improve the rational use of human serum albumin(HSA)in cancer patients by the interventions of clinical pharmacists.Methods Literature search of HSA was performed by clinical pharmacists for clinical indications and appropriate usage.The HSA use protocol was implemented by clinical pharmacists and related clinical experts.The protocol adaptation was reinforced by clinical pharmacists.Results The rate of the rational use of HSA has been improved.Conclusion Clinical pharmacists play an important role in the clinical rational use of HSA based on evidence-based pharmacy.

Evaluation on the clinical utilization of human serum albumin in ICU patients / 药学实践杂志

Objective To evaluate the utilization of human serum albumin (HSA ) in intensive care unit (ICU ) to pro-mote rational use of HSA clinically .Methods Data were collected from the patients received HSA therapy during the period of January 1 ,2015 to December 31 ,2015 .The indications and usage of HSA were analyzed statistically .Results 416 bottles of HSA were administered to 64 patients .The average dose was 62 .5g per patient .The most popular indication was for hypopro-teinemia (39 .1% ) followed by encephaledema ,craniocerebral trauma ,shock and tumors .Before the HSA therapy ,36 patients (56 .3% ) had albumin level of 15-25 g/L and 23 patients (35 .9% ) of 25-35 g/L .Conclusion HSA is widely used in ICU for different indications .Some misuses still exist .Guidelines for proper use of HSA are needed to guarantee its rational use .HSA should be used strictly following these guidelines .

Spectroscopic study on interaction of quercitrin with human serum albumin / 中草药

Objective: To study the interaction of quercitrin with human serum albumin (HSA) and the influence of glucose. Methods: To investigate the interaction mechanism between quercitrin and HSA by spectroscopic method; to calculate the binding constants, binding sites, and binding distance according to double logarithmic plot and Föster's energy transfer theory, respectively; to explain the type of interaction force between quercitrin with HSA by thermodynamic parameters; to discuss the conformation change of HSA via synchronous fluorescence spectra. Results: The fluorescence quenching mechanism of quercitrin to HSA was static quenching; The binding constants and the number of binding sites decreased with the increasing of temperature and glucose; The distance between the donor and acceptor was less than 7 nm; The hydrophobic forces played a major role in stabilizing quercetrin and HSA complex; The binding reaction had changed the micro-environmention of tryptophan residues. Conclusion: Quercetrin could bind with HSA and change the conformation of HSA; The physiological concentration of glucose increases the binding constants and the number of binding sites of quercetrin with HSA.

A Study on Pulmonary Extraction Rates of Biogenic Amines and Permeability of Serum Albumin in Dogs with Experimental Acute Respiratory Failure / 대한마취과학회지

The extraction rates of biogenic amines such as 5-hydroxytryptamine(5-HT) and norepinephrine(NE) in pulmonary endothelium, and the permeability of human serum albumin(HSA) to pulmonary epithelium were measured in experimental adult respiratory distress syndrome(ARDS), in order to evaluate their usefulness for the early recognition of ARDS. Sixteen mongrel dogs(body weight, 13+/-0.9 kg) were divided into 3 groups; Oleic acid 0.06 ml/kg was injected to 6 dogs(M group) and oleic acid 0.12 ml/kg to 6 dogs(S group). Four dogs were used as a control group. The extraction rates(%) of 14C-5-HT and 3H-NE, the blood concentration of (99m)Tc-HSA, hemodynamic changes and changes of arterial gas profile were measured and compared among three groups. In control group with 100% oxygen ventilation, the extraction rates of 14C-5-HT, 3H-NE and the blood concentration of 99mTc-HSA were not changed. In M group, the extraction rate(%) of 14C-5-HT was decreased from 61.5+/-3.1 to 43.8+/-5.2 in 10 minutes, and such decreased extraction rate(%) was maintained for 2 hours. The extraction rate(%) of (3)H-NE was decreased from 32.3+/-3.6 to 19.5+/-2.5 in 10 minutes. In S group, the extraction rate(%) of 14C-5-HT was decreased from 60.9+/-5.1 to 23.2+/-5.7 in the first 10 minutes, and the extraction rate(%) of H-NE was decreased from 30.1+/-4.3 to l3.1+/-1.9 in 10 min, and decreased slowly thereafter. The blood concentration of 99mTc-HSA was decreased significantly in M group and more in S group compared with control group during two-hour observation. These results suggest that measuring extraction rates of biogenic amines couid be applied for early recognition of ARDS, however, the change of blood 99mTc-HSA concentration could not be applied for early recognition of ARDS, because it has poor correlation to the progression of respiratory failure.

Non-covalent binding between tectoridin and plasma proteins by electrospray ion trap mass spectrometry / 中草药

Objective To study the non-covalent binding between the tectoridin(TE) and plasma proteins.Methods The molecular weights of TE,human serum albumin(HSA),?1-acid glycoprotein(AAG) and the protein-drug complexes were measured by the electrospray ion trap mass spectrometry(ESI-MS).The maximum stoichiometric ratios were obtained according to the molecular weight change of the complexes before and after binding reaction.The binding constants(K) of the complexes were calculated by the Scatchard equation.The main sorts of binding force of the complexes were deduced according to the relationship between the reaction temperature and the thermodynamic parameters(?H and ?S).Results The K of the complexes were 1.914?104 mol/L for TE-HSA and 5.893?104 mol/L for TE-AAG,and the number of binding sites were 7.8 and 3.3,respectively.The main sorts of binding force between TE-HSA or TE-AAG were static-electricity gravitation.Conclusion ESI-MS is a good method for studying of the TE-protein non-covalent binding with some advantages in sensitivity,high-speed,and accuracy.