Glycoproteins blood serum

Madera, M., Mechref, Y, Klouckova, I., and Novotny, M. V., Semiautomated high-sensitivity profiling of human blood serum glycoproteins through lectin preconcentration and multidimensional chromatography/tandem mass spectrometry. Journal of Proteome Research 5(9), 2348-2363, 2006. 

Application of Lectins for the Detection of Ab to Viral Glycoproteins in the Blood Serum... 

Fish living in Arctic and Antarctic waters may encounter temperatures as low as -1.9°C. The freezing point depression provided by dissolved salts and proteins in the blood is insufficient to protect the fish from freezing. As winter approaches, they synthesize and accumulate in their blood serum a series of eight or more special antifreeze proteins.a d One type of antifreeze glycoprotein from winter flounder contains the following unit repeated 17-50 times. 

Antifreeze glycoprotein is a collective name for a family of at least eight closely related glycoproteins that account for a major fraction of the protein in the blood serum of certain Antarctic fishes. The glycoproteins have been numbered according to the order of migration of... 

The glycoproteins are easily separated from blood serum by sequential purification using ion-exchange chromatography and gel-exclusion columns. They can also be separated or further purified from other constituents by trichloroacetic acid-acetone precipitation of most other proteins, salt fractionation, and electrophoresis in borate buffer. All eight glycoproteins have been purified and separated from one another. 

Initial studies on the polar cod blood serum have shown that its antifreeze protein is a glycoprotein with most properties similar to those from the Antarctic species T. borchgrevinki. Both active and inactive components were obtained. The active components had the same ratios of alanine to threonine (approximately 2 1) as found in the Antarctic glycoproteins and the same contents of galactosamine and galactose. No other amino acids were found. In contrast to the comparatively low antifreeze activity of the saffron cod reported by Raymond and co-workers, the AFGP from the polar cod had an antifreeze activity similar to that from the Antarctic species. 

The H NMR spectra of the synovial fluid of a female patient with seronegative erosive rheumatoid arthritis and of another female patient with sarcoidosis and independent inflammatory osteoarthritis were followed over the course of several months and standard clinical tests were performed on paired blood serum samples taken at the same time. It was found that the synovial fluid levels of triglyceride CH3, CHj and CH, glycoprotein N-acetyl signals and creatinine all correlated well with one another, and with standard clinical measures of inflammation. The correlation of disease state with creatinine level is of particular interest, and the altered triglyceride composition and concentration in osteoarthritis were suggested as potential markers for the disease in synovial fluid. ... 

The transferrins are a class of iron-binding glycoproteins which have been found in the blood serum of a variety of vertebrates and are presumably also present in moth hemolymph [see (74) and references therein], These proteins would appear to mediate the absorption and distribution of iron (75), and could play some role in the movement of carbon dioxide in the body (76). Proteins of similar characteristics, lactoferrin and conalbumin, have been isolated from milk and avian egg white respectively. It has been proposed (77) that conalbumin could prevent bacterial contamination of the egg yolk by removing free iron. A similar bacteriostatic action could be performed by lactoferrin in milk, and it is possible that this protein is involved in controlling the intestinal flora in infants (78). 

It has been suggested that in some forms of the disease there may be an elevated sequestration of caeruloplasmin by the parenchymal cells of the liver, leading to a low level of this glycoprotein in serum and a heavy load of copper on the liver. Copper in blood will increasingly come to bind to those proteins for which it has a lower affinity than for caeruloplasmin. Some copper reaches the brain, for which it is intensely toxic. 

The whole sample was then injected onto the chiral column, 10 cm long, 4.0 mm I.D., packed with silica gel particles, 5 pm in diameter, bonded with a,-acid glycoprotein (AGP). The results obtained are shown in figure 11.2. The separation ratio between the enantiomer pair is 1.23. Chromatogram (A) is the separation of a 50 ng sample of the racemic pair. Chromatogram (B) is from a blood serum sample taken 4 hours after the oral administration of 120 mg of racemic Verapamil. Chromatogram (C) is from a blood serum sample taken 15 min after the intravenous infusion of 15 mg of racemic Verapamil. It is clear that this type of analysis will allow an accurate pharmokinetic study of the relative biochemical degradation or excretion of the two enantiomers. 

Gas Chromatography Analysis of Sugars in Glycoproteins of Blood Serum Chem. Zvesti 31(1) 87-91 (1977) CA 88 71075f... 

The occurrence and composition of the glycoproteins in human blood serum have been reviewed by Winzler (5). Evidence for the existence of at least four such materials has been obtained by Schmid 79). One of these is present in serum to the extent of 0.5 % and is the principal glycoprotein of the ai-globulin fraction. 

A glycoprotein resembling the ai-glycoprotein of blood serum has been isolated from the urine of patients with proteinuria 85). It contains D-glu-cosamine, D-mannose, and D-galactose as its carbohydrate constituents. Its electrophoretic behavior and immunochemical reactions greatly resemble those of the ai-glycoprotein isolated by Schmid. It is clearly not the glycoprotein isolated from normal urine by Tamm and Horsfall. 

The water-soluble globular protein fraction can be separated electrophoretically into a-, P- and y-Uvetins (Table 11.9). These have been proven to correspond to chicken blood serum proteins, i. e. semm albumin, a2-glycoprotein and y-globulin. 

Sialoglycoproteins occur in avian blood serum and in erythrocyte membranes. The sera of chicken, turkey, goose, and duck contain sialic acids as NeuSAc with less than 10% as Neu5Gc. No 0-acetylated derivatives were reported (Faillard and Cabezas 1963, DzuiYNSKAct al. 1969). A hepatic receptor, responsible for the removal of avian serum glycoproteins contains sialic acid, which in contrast to the analogous receptor in mammalian liver tissues remains active after removal of the sialic acid by sialidase (LuNNEvand Ashwell 1976, Kawasaki and Ashwell 1977). 

Hudgin, R. L., and Schachter, H., 1971, Porcine sugar nucleotide glycoprotein glycosyl-transferases I. Blood serum and liver sialyltransferase. Can. J. Biochem. 49 829-837. 

There are several positive factors using BSA in the basolateral medium. First, it mimics the in vivo situation where the circulating blood provides an excellent base for sink conditions due to a large volume and content of serum proteins such as albumin (serum protein content and alpha-glycoproteins) [108]. Second, serum albumin hinders adsorption onto plastic surfaces and filters and thereby stops the... 

---