Albumin benefit, serum level

Subscribe to a FREE alternative healing newsletter.
April 16 2016 by Ray Sahelian, M.D.
 

Albumin is the term for a group of proteins making up close to 60% of the protein in blood plasma. Albumin proteins are important in regulating blood volume by maintaining the osmotic pressure of the blood compartment. Albumin proteins are important for transporting fatty acids, thyroid hormones, some steroid hormones, and other substances in the bloodstream.

Serum albumin blood test
The albumin blood test measures the amount of albumin in serum, the clear fluid portion of blood. The albumin blood test is done to help determine if a patient has liver disease or kidney disease, or if not enough protein is being absorbed by the body.

Albumin food source
Albumin is found in many foods, predominantly in egg white and milk.

Stroke treatment
High-dose albumin appears to be safe and therapeutic if administered soon after onset of an acute ischemic cerebral infarction. When administered along with tissue-type plasminogen activator (tPA), the efficacy of albumin is further enhanced. Stroke 2006.

Diagnosis, biomarker
J Pharmacology Biomed Anal. 2014. Mass spectrometric characterization of human serum albumin dimer: A new potential biomarker in chronic liver diseases. Human serum albumin (HSA) undergoes several structural alterations affecting its properties in pro-oxidant and pro-inflammatory environments, as it occurs during liver cirrhosis. These modifications include the formation of albumin dimers. Although HSA dimers were reported to be an oxidative stress biomarker, to date nothing is known about their role in liver cirrhosis and related complications. Additionally, no high sensitive analytical method was available for HSA dimers assessment in clinical settings. Thus the HSA dimeric form in human plasma was characterized by mass spectrometry using liquid chromatography tandem mass spectrometry (LC-ESI-Q-TOF) and matrix assisted laser desorption time of flight (MALDI-TOF) techniques. N-terminal and C-terminal truncated HSA, as well as the native HSA, undergo dimerization by binding another HSA molecule. This study demonstrated the presence of both homo- and hetero-dimeric forms of HSA. The dimerization site was proved to be at Cys-34, forming a disulphide bridge between two albumin molecules, as determined by LC-MS analysis after tryptic digestion. Interestingly, when plasma samples from cirrhotic subjects were analysed, the dimer/monomer ratio resulted significantly increased when compared to that of healthy subjects. These isoforms could represent promising biomarkers for liver disease. Additionally, this analytical approach leads to the relative quantification of the residual native HSA, with fully preserved structural integrity.