Binding Properties of Glycosylated Albumin and Acetaldehyde Albumin

Glucose and acetaldehyde react covalently with albumin to form the post-translationally modified group of proteins, the glycosylated albumins and the acetaldehyde albumins, respectively. This study contrasts the binding ability of a major acetaldehyde albumin fraction synthesized in vitro with glycosylated albumin. A microdialysis rate method, using either [14C]monoacetyldiaminodiphenyl sulfone (MADDS), a deputy ligand for bilirubin, or [14C]diazepam, was employed to evaluate binding at these two sites. Our results indicate that prolonged exposure of purified human serum albumin to acetaldehyde results in a major acetaldehyde albumin fraction that lacks the ability to bind MADDS and diazepam. This fraction migrates identically to albumin on SDS polyacrylamide gel electrophoresis, but exhibits microheterogeneity with a more acidic pI band as seen on analytical isoelectric focusing. We suggest that altered drug binding in alcoholics may be partially explained by altered binding ability of acetaldehyde albumins.     

Quantitative Determination of Albumin Dimer in Albumin Preparations by Combined Starch-Gel Electrophoresis and Immunoprecipitation

Abstract. A method is described for albumin dimer determination. The method is based upon an electrophoretic separation of albumin dimer from the monomer in starch gel with a subsequent immunochemical diffusion and precipitation of the albumin components in agarose gel containing antibodies. The precipitation zones are measured and compared with those of albumin monomer standards. A factor for converting monomer to dimer has furthermore been established.     

Reduction of Aluminium Concentration in Albumin Products

The aluminium concentration in albumin products has been reduced to ≥100 ppb by an anion exchanger treatment. Furthermore, we have found that this low aluminium concentration in albumin products has been maintained for extensive periods of time, when they are stored in de-alkalized soft glass containers.     

缺血修饰白蛋白临床应用研究进展

缺血修饰白蛋白(ischemia modified albumin,IMA)是近年来发现的新的心肌缺血标志物,具有极高的敏感性,能在心肌缺血的早期阶段检出,有助于心肌缺血的诊断和急性冠脉综合征的危险分层.现简要介绍近年来IMA临床应用的研究进展.     

Anti-I Autoantibody Acting Preferentially in Albumin

Abstract. An anti-I autoantibody is reported which acted almost exclusively in albumin and was at first mistaken for the antibody responsible for the albumin autoagglutinating property, which is dependent on the presence of sodium caprylate added to albumin as a stabiliser. It is recommended that all sera thought to exhibit non-specific autoagglutination in albumin be carefully investigated for blood group specificity.     

缺血性卒中的白蛋白治疗

白蛋白是血浆中含量最多、分子量最小、溶解度大、功能较多的一种蛋白质。白蛋白不易透过血脑屏障,具有重要的结合转运功能,能通过调节胶体渗透压消除或减轻脑水肿,亦可结合体液中的毒性成分使之失效,还能转运营养成分和有关治疗药物,发挥广泛的临床治疗作用。近年来,人们发现白蛋白在脑缺血中有着显著的保护作用。     

Albumin regeneration in liver support-comparison of different methods

Albumin is the most abundant human plasma protein. Among many other functions it is an important transporter of hydrophobic internal and external substances such as intermediate and end products of metabolism and drugs. In liver failure the albumin binding capacity is decreased because of a disproportion between available albumin molecules caused by decreased hepatic synthesis and hydrophobic toxins because of decreased hepatic clearance. The resulting increase in plasma and tissue concentrations of these substances is associated with multiple organ dysfunctions frequently seen in severe liver failure. The scope of the present article is to compare different liver support strategies with regard to their ability to regenerate the patients albumin pool by removing albumin-bound toxins. Most prominent technique in this group is the molecular adsorbent recirculating system (MARS). It will be compared with single pass albumin dialysis (SPAD), fractionated plasma separation and adsorption system (FPSA, Prometheus), and plasma perfusion/bilirubin adsorption with special regard to efficacy and selectivity.     

Albumin excretion and vascular deaths in NIDDM

Summary Non-insulin-dependent diabetes mellitus (NIDDM) is associated with premature mortality, generally thought to be exaggerated in patients with microalbuminuria. This prospective 8-year follow-up study aimed to determine outcome, mortality and cause of death in NIDDM patients with abnormal urinary albumin excretion compared to those with normal albumin excretion. We recruited 153 NIDDM patients with abnormal urinary albumin excretion and 153 control subjects with albumin excretion within the normal non-diabetic range, matched for age, sex and duration of diabetes, from three University hospital diabetic clinics in Newcastle upon Tyne. The outcome measures were status at follow-up, mortality and cause of death. Subjects with abnormal albumin excretion had a significantly higher 8-year mortality than matched control subjects (Odds Ratio 1.47, p=0.02; 108 vs 66 per 1000 person years follow-up, p<0.001). This difference was seen at all levels of abnormal albumin excretion, from just outside the normal range (10.6–29.9 g/min: 104 vs 61 per 1000 person years follow-up, p<0.001) to more conventional definitions of microalbuminuria (30 g/min: 111 vs 71 per 1000 person years follow-up, p<0.01). Those with abnormal albumin excretion had an excess of vascular deaths compared to matched control subjects (Odds Ratio 1.70, p = 0.009), again at different levels of albumin excretion (10.6–29.9 g/min p<0.01, 30–150 g/min p<0.05). On multivariate analysis, age, initial ischaemic heart disease and initial albumin excretion rates were independent predictors of death from all causes. Even a minor elevation of albumin excretion above the normal non-diabetic range is associated with excess mortality from vascular causes in NIDDM.Abbreviations NIDDM Non-insulin-dependent diabetes mellitus - AER albumin excretion rate - SBP systolic blood pressure - DBP diastolic blood pressure - CI confidence interval - MAP mean arterial pressure