Topic
Serum albumin
About: Serum albumin is a research topic. Over the lifetime, 16337 publications have been published within this topic receiving 516395 citations. The topic is also known as: blood albumin & ANALBA.
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TL;DR: The present study has successfully used this principle to detect alterations in blood supply to various regions of the lung as a result of certain diseases, using chromiumlabeled albumin as a label for the macro-aggregated albumin.
Abstract: THE RATE OF ACCUMULATION of a substance in any region of the body is directly proportional to the blood flow to the region, provided the substance is completely removed from the blood and is not metabolized during the period of observation. In the present study, we have successfully used this principle to detect alterations in blood supply to various regions of the lung as a result of certain diseases. The studies were made possible by the development of a new radiopharmaceutical, labeled macro-aggregated albumin (MAA), which has been found to be both safe and effective. Materials and Methods In the initial studies radiodine (I 131 ) was employed as a label for the macro-aggregated albumin. Subsequently we have used chromiumlabeled albumin, because radioactive chromium (Cr 51 ) emits a mono-energetic gamma ray (320 kilo electron volts) that is preferable for scintillation scanning. In addition, the absence of beta emission decreases the radiation
178 citations
TL;DR: HSA structure was less perturbed by polyamine analogues compared to those of the biogenic polyamines, and the protein secondary structure showed major alterations, indicating partial protein unfolding upon polyamine interaction.
178 citations
TL;DR: Sorbol, at concentrations from 0 to 2 M, led to the progressive restoration of BSA volume and compressibility values, as well as a substantial recovery of its original alpha-helix content, implying that the compressibility variation observed reflects the conformational changes during the transition.
178 citations
TL;DR: On exposure to increasing concentrations of insulin, myoglobin, protein A, peroxidase, serum albumin, galactosylated serumalbumin, lactoferrin, transferrin, catalase, low-density lipoprotein, ferritin, and polymeric IgA, protein binding was a saturable process.
Abstract: We prepared homogeneous populations of colloidal gold particles of various sizes. These were analyzed for size distribution and number of particles per unit volume. On exposure to increasing concentrations of insulin, myoglobin, protein A, peroxidase, serum albumin, galactosylated serum albumin, lactoferrin, transferrin, catalase, low-density lipoprotein, ferritin, and polymeric IgA, protein binding was a saturable process. Using serum albumin, we verified that a reversible equilibrium was reached within 15 minutes. Scatchard analysis of the interactions between all of these proteins and the gold particles resulted in a single component, linear relation. For a given particle size, the number of binding sites for various proteins was inversely proportional to their molecular weight. Conversely, when the size of particles was varied, the number of binding sites was directly proportional to the average area of each gold particle. All results are compatible with a monomolecular shell of protein surrounding the particle at saturation, the binding capacity being inversely proportional to the projection area of the protein. We present direct morphological evidence for this model. The affinity of the various proteins for the colloid also increased with molecular weight, and was not related to the protein isoelectric point. For globular proteins, the monomolecular shell model makes possible prediction of the number of molecules that will saturate a gold particle, if the average diameter of the gold particles and the molecular weight of the protein are known.
178 citations
177 citations