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Results for “Orosomucoid”

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At least 19 recordsLinked to original sources
PubMed1976

Serum orosomucoid in ulcerative colitis: its relation to clinical activity, protein loss, and turnover of albumin and IgG.

Serum orosomucoid was compared with clinical activity, routine laboratory tests, intestinal protein loss, and albumin and IgG turnover in 22 cases of ulcerative colitis. Serum orosomucoid was well correlated with clinical activity, haemoglobin and leucocyte counts were not. A significant correlation was present between serum orosomucoid and intestinal protein loss (gastro-intestinal 59Fe-iron dextran clearance), serum albumin, fractional catabolic rates of albumin, and IgG and IgG synthesis rate. No correlation was found between serum orosomucoid and albumin synthesis rate or serum IgG. It is concluded that serum orosomucoid is a highly reliable indicator of disease activity in ulcerative colitis.

Adolescent↗
PubMed1978

Kinetics of uptake and activity in mouse liver of glutaminase coupled to desialated orosomucoid.

Desialised orosomucoid (alpha-1-acidic glycoprotein) was coupled to Pseudomonas 7A glutaminase-asparaginase by glutaraldehyde, iodinated and injected into mice. The half-life of radioactivity and glutaminase activity in plasma was about 7 min. Radioactivity and glutaminase activity in the liver reached a peak at about 20 min. The radioactivity in liver then declined with a half-life of about 20 min. Enzyme activity in liver declined with a half-life of about 10 min. The ratio of enzyme activity to radioactivity was lower in the liver than in plasma at all times during the experiment, indicating rapid hepatic inactivation of the enzyme. Uptake into the liver could be blocked by excess desialised orosomucoid. Glutamine levels in the liver were about 10% of normal for 44 min but returned to 50% of normal by 93 min. Intestines, kidney and spleen failed to exhibit any appreciable uptake of desialated orosomucoid glutaminase-asparaginase.

Animals↗
PubMed1978

Plasma clearance of glycoproteins with terminal mannose and N-acetylglucosamine by liver non-parenchymal cells. Studies with beta-glucuronidase, N-acetyl-beta-D-glucosaminidase, ribonuclease B and agalacto-orosomucoid.

Glycoproteins having mannose and/or N-acetylglucosamine in the terminal non-reducing position [Stockert, Morell & Scheinberg (1976) Biochem. Biophys. Res. Commun. 68, 988--993], and various lysosomal enzymes [Stahl, Schlesinger, Rodman & Doebber (1976) Nature (London) 264, 86--8] are rapidly cleared from plasma by the liver after intravenous administration. A liver cell-separation technique was used to determine the cellular localization of 125I-labelled beta-glucuronidase, ribonuclease B, agalacto-orosomucoid and asialo-orosomucoid. On a specific readioactivity basis, all ligands except 125I-labelled asialo-orosomucoid were enriched in the non-parenchymal cell fraction. Isolated cells, fixed and stained for beta-glucuronidase or N-acetyl-beta-D-glucosaminidase activity after intravenous injection of the enzymes, showed enrichment in the non-parenchymal cell fraction (probably Kupffer cells). After uptake by the non-parenchymal cells, liver lysosomal beta-glucuronidase and N-acetyl-beta-D-glucosaminidase showed degradation half-times of 2.2 and 0.4 days respectively.

Acetylglucosamine↗
PubMed1978

Identification of a breast tumor-associated orosomucoid by concanavalin A affinity chromatography.

Con A-Sepharose affinity chromatography was utilized to examine the glycoproteins in phosphosaline extracts of normal and breast tumor tissues and breast patient sera. In extracts of normal breast tissue, normal sera and patient sera, all glycoproteins were eluted from the Con A-Sepharose with a linear gradient of 0.0-0.5 M alpha-methylmannose. Using breast tumor extracts, a glycoprotein peak which could not be eluted as with normal tissue extracts was observed. This tightly-binding peak could be eluted from the Con A-Sepharose with acetate buffer containing 1.0 M KCl. Polyacrylamide electrophoresis of this tightly-binding glycoprotein peak revealed one major glycoprotein and four minor glycoproteins. The major glycoprotein obtained from electrophoresis represented about 60% of the Con A-Sepharose tightly-binding protein and reacted with antiserum to human orosomucoid (alpha 1-acid glycoprotein). All glycoproteins isolated from tumor tissue extracts appeared to represent normal serum constituents as they were retained on an immunoadsorbent containing antibodies to normal serum proteins. The possible significance of the isolated tumor-associated orosomucoid is discussed.

Adenocarcinoma↗
PubMed1977

The effect of chemical treatments of albumin and orosomucoid on rate of clearance from the rat bloodstream and rate of pinocytic capture of rat yolk sac cultured in vitro.

Portions of a 125I-iodinated bovine serum albumin preparation were exposed to freezing, acetic acid (pH 3.5, 3.0 or 2.5), urea or formaldehyde, and the effect of these treatments on the rates of pinocytic uptake by yolk sacs from 17.5-day-pregnant rats cultured in vitro and of clearance from the rat bloodstream were studied. Uptake of albumin by the yolk sac was followed by rapid release of [125I]iodo-L-tyrosine into the culture medium. Similarly clearance of albumin in vivo was accompanied by the appearance of trichloroacetic acid-soluble radioactivity in the bloodstream. In both systems the rates of uptake of modified albumin preparations formed a series: formaldehyde or urea greater than acetic acid greater than freezing. The increased rates of uptake of modified albumin preparations could not be ascribed to the formation of aggregates nor, in the yolk-sac system, to an increase in the rate of pinosome formation. It is concluded that the various treatments to which the albumin was subjected increase to varying degrees the affinity of the albumin molecule for binding sites on that region of the plasma membrane from which pinocytic vesicles are formed. Some comparable experiments with native and desialylated human orosomucoid indicate that the rat yolk-sac epithelial cells do not possess the recognition system for uptake of asialoglycoproteins that exists on the surface of hepatic parenchymal cells.

Acetates↗
PubMed1977

Orosomucoid contents of pleural and peritoneal effusion of various etiologies.

Orosomucoid and the contents of seven other proteins were determined by radial immunodiffusion in sera and in pleural or peritoneal fluids of 66 patients. No significant difference between concentration of individual proteins in effusions of neoplastic origin and those of nonneoplastic inflammatory origin was found. In noninflammatory fluids, the protein concentrations were lower, but their distribution was similar to distributions in the other fluids tested. These findings support the view that the protein content of effusions reflects changes in vascular permeability.

Ascitic Fluid↗
PubMed1975

C3, GBG, orosomucoid and haptoglobin polymorphisms. Improved staining methods.

C3, GBG, and orosomucoid polymorphisms were electrophoresed in a high-voltage agarose method which permitted the typing of 15-20 samples. The increased sensitivity of the dye Coommassie blue was used to stain the protein, and yielded higher resolution than amido black. The typing of haptoglobin samples, was facilitated by devising a method which utilizes the peroxidase activity of the haptoglobin-hemoglobin complex with 90-tolidine and hydrogen peroxide as substrates and 4-chloro-1-naphthol as coupler.

Complement System Proteins↗
PubMed1976

[Alpha-1-antitrypsin, orosomucoid, transferrin and alpha fetoprotein in the amniotic fluid, Changes in concentration in normal and pathologic pregnancies].

In this article, which is a preliminary report, the authors determined amniotic fluid levels of alpha-I-antitrypsin, orosomucoid, transferrin and alpha-fetoprotein during complicated pregnancies with gestational ages of 31 to 42 weeks. These levels were compared with those observed during normal pregnancies. The clinical value of the variations of the glycoprotein levels is discussed.

Amniotic Fluid↗
PubMed1978

Leukocyte surface origin of human alpha1-acid glycoprotein (orosomucoid).

Specific antibodies against human alpha1-acid glycoprotein reacted with human lymphocytes, granulocytes, and monocytes. The antigen on the leukocytes is an externally located integral membrane glycoprotein which is made by the cells and has an apparent mol wt of 52,000. It is released from cells in vitro to the culture medium. The mol wt of the soluble fragment is 41,000, which corresponds to that of alpha1-acid glycoprotein in serum and urine. Peptide mapping confirmed that the main part of the cellular membrane antigen consists of alpha1-acid glycoprotein with an additional, probably hydrophobic fragment. This finding may partially explain the increase in the serum levels of alpha1-acid glycoprotein observed in many disorders involving leukocyte proliferation. In addition, the known sequence homology of alpha1-acid glycoprotein with immunoglobulins can now be more easily understood by their origin in similar cell types.

Antigens, Surface↗