Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The purified ricinotoxin from Ricinus communis L. seeds appears to be a glycoprotein. Either paper or gas-liquid chromatographic methods indicate that only mannose and N-acetyl-glucosamine are present in significant amounts. Quantitative determination shows that one mole of ricinotoxin contains 15 mannose residues and 8 N-acetyl-glucosamine residues.
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PMID:Characterization, composition and determination of the sugars in ricinotoxin from Ricinus communis L. seeds. 74 70

A radioimmunoassay was developed for murine lactoferrin (LF), a non-heme, iron-binding glycoprotein which appears to be a specific biochemical marker of differentiation in several cell types. Lactoferrin was labeled with 125I by the chloramine-T method to yield a product having 20 muCi/mug protein and an isotope incorporation of 0.6 atoms of 125I per molecule. Separation of bound and free lactoferrin was accomplished by either of two procedures, a double-antibody technique or precipitation in the presence of 50% saturated ammonium sulfate. The entire assay, including counting, was accomplished in less than 2 days and had a lower limit of sensitivity and a range of 1 ng/ml and 1-32 ng/ml, respectively, using rabbit antiserum in a dilution of about 1:10,000. The binding between LF and rabbit antiserum exhibited two association constants having values of 1.8 x 10(11) and 1 x 10(9) l/mole. The assay was specific for lactoferrin and no cross-reactivity was observed with transferrin, a similar non-heme, iron-binding glycoprotein. Human lactoferrin specifically reacted with anti-mouse lactoferrin, but the binding was approximately 8000 times weaker than observed with mouse lactoferrin. Values for lactoferrin in milk and bone marrow granulocytes were obtained which agreed with levels obtained using other methods.
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PMID:Radioimmunoassay for murine lactoferrin, a protein marker of myeloid and mammary epithelial secretory cell differentiation. 83 25

The properties of colchicine uptake into Chinese hamster ovary cells were examined and found to be consistent with an unmediated diffusion mode. This uptake was stimulated several fold by metabolic inhibitors. The activation energy of colchicine uptake was found to be 19 kcal per mole; a similar value was obtained in cells stimulated by cyanide. Drug resistant mutants with greatly reduced colchicine permeability have been isolated. They displayed a pleiotropic phenotype, being cross-resistant to a variety of unrelated compounds. The basis of this pleiotropy was due also to reduced drug permeability. Examination of the lipids and fatty acids of parental and mutant cell membranes revealed no major differences. However, a 170,000 dalton surface glycoprotein was observed to be associated with colchicine resistance. This glycoprotein was postulated to be a modulator of drug permeability. All these data are consistent with the concept that mammalian cells are able to regulate the permeation of drugs entering by an unmediated diffusion process.
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PMID:Altered drug permeability in mammalian cell mutants. 89 49

Four major glycoproteins were extracted by dilute salt solution from procine mitral valvular tissue. Two of these major glycoproteins, procine valve glycoprotein I and porcine valve glycoprotein III, were isolated and purified by fractionation of salt extract with ammonium sulfate followed by column chromatography on DEAE-cellulose. The purified glycoproteins appeared to be homogeneous by polyacrylamide disc electrophoresis in several buffer systems, and by Sephadex filtration. The porcine valve glycoprotein I has a molecular weight of approximately 120000. Isoelectric focusing yielded a single band, pI = 5.8. The glycoprotein contained large amounts of acidic amino acids, and amide nitrogen. The carbohydrate moiety was composed of fucose, mannose, galactose, glucose, glucosamine, and galactosamine in the molar ratio of 5:10:15:12:7:2 per mole of glycoprotein. The second major glycoprotein, porcine valve glycoprotein III, has an approximate molecular weight of 72000. This glycoprotein gives two bands upon analytical isoelectric focusing with isoelectric points of pI = 4.1 and 4.3. Porcine valve glycoprotein III contained large amounts of acidic amino acids and low amounts of amide nitrogen. Its carbohydrate moiety was composed of glucose, galactose, mannose, fucose, glucosamine, and sialic acid in the ratio of 3:3:2:1:4:1 mol/mole of glycoprotein. This glycoprotein was similar to a glycoprotein preparation isolated from porcine aortic intima by P.V. Wagh and B.I. Roberts (1972), Biochemistry 11, 4222.
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PMID:Purification and chemical characterization of salt-extractable glycoproteins from porcine mitral valve. 93 28

Coagulation Factor VII from bovine plasma is a glycoprotein containing a single peptide chain. The NH2-terminal sequence of Ala-Asx-Gly-Phe-Leu- is homologous with the NH2 termini of prothrombin, Factor IX, and the light chain of Factor X. Factor Xa in the presence of calcium ions and phospholipid cleaves Factor VII at an Arg-Ile bond in the sequence Arg-Ile-Val-Gly-Gly-, producing a two-chain molecule with at least 85 times the coagulant activity of single-chain Factor VII and a new NH2-terminal sequence homologous with the corresponding chains of thrombin, Factor IXa and Factor Xa. A second slower cleavage at an Arg-Gly bond destroys Factor VII activity. Bovine Factor VII, unlike prothrombin, Factor IX, and Factor X, is rapidly inhibited by diisopropylphosphorofluoridate (iPr2PF). [3H]iPr2PF is readily incorporated into one-chain, two-chain, and three-chain forms of Factor VII up to ratios of approximately 0.9 moles of [3H]diisopropylphosphate per mole of protein. The radioactive peptides generated from each form of [32P]iPr2PF-inhibited Factor VII by tryptic and thermolytic digestion were found to migrate together on paper electrophoresis. This indicates that the iPr2PF is incorporated stoichiometrically into the same specific site in each form.
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PMID:Mechanism of activation of bovine factor VII. Products of cleavage by factor Xa. 95 65

Protected disaccharides were the only products that could be isolated after condensation of 3, 4, 6-tri-O-acetyl-2-deoxy-2-diphenoxyphosphoramido-alpha-D-glucopyranosyl bromide or 2-acetamido-3, 4, 6-tri-O-acetyl-2-deoxy-alpha-D-glucopyranosyl chloride with benzyl 2, 4-di-O-benzyl-beta-D-galactopyranoside. On the other hand, reaction of 2-methyl-(3, 4, 6-tri-O-acetyl-1, 2-dideoxy-alpha-D-glucopyrano)-[2', 1': 4, 5]-2-oxazoline (6 moles) with the same galactopyranoside (1 mole) gave benzyl 3, 6-di-O-(2-acetamido-3, 4, 6-tri-O-acetyl-beta-D-glucopyranosyl)-2, 4-di-O-benzyl-beta-D-galactopyranoside, which was converted, by alkaline methanolysis followed by hydrogenolysis, to the title compound. This appears identical with an oligosaccharide previously obtained through degredation of a blood-group A glycoprotein from hog gastric mucin.
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PMID:The synthesis of 3, 6-di-O-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-D-galactose, a branched trisaccharide reported as a hydrolysis product of blood-group substances. 112 50

Thrombospondin is a large, trimeric glycoprotein secreted by activated platelets and growing cells. Thrombospondin copolymerizes with fibrin during blood coagulation and deposits in extracellular matrix. We found that thrombospondin is a slow (rate constant approximately 6.3 x 10(3) M-1 sec-1), tight-binding (Kd < 10(-9) M) inhibitor of plasmin as determined by loss of amidolytic activity, loss of ability to degrade fibrinogen, and decreased lysis zones in fibrin plate assays (Biochemistry 31: 265-269, 1992). Thrombospondin also slowly inhibits urokinase plasminogen activator. The lysis zone when urokinase is put on fibrin plates made from whole plasma is less if thrombospondin is present. The stoichiometry of inhibition is approximately one mole plasmin:one mole thrombospondin trimer, a somewhat surprising result considering the trimeric nature of thrombospondin. These results indicate that thrombospondin is an important regulator of fibrinolysis and degradation of extracellular matrix, particularly when these processes are initiated by urokinase and even when other inhibitors of fibrinolysis are present.
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PMID:Modulation of fibrinolysis by thrombospondin. 130 73

Surfactant protein D (SP-D), a multimeric calcium-dependent lectin isolated from pulmonary alveolar lavage, has been previously shown to interact reversibly with crude surfactant [Persson et al. (1990) J. Biol. Chem. 265, 5755-5760]. In this study, SP-D is shown to interact reversibly with a preparation of organelles enriched in lamellar bodies, in a manner inhibited by calcium-chelating agents and by competing saccharides. An interaction with an endogenous glycoprotein could not be identified by electrophoresis of surfactant or lamellar body-associated proteins followed by electrotransfer of the separated proteins to nitrocellulose and then probing with radioiodinated SP-D via lectin overlay. Separation of the surfactant or lamellar body lipids on two-dimensional thin-layer chromatography (2D-TLC) followed by probing with radioiodinated SP-D via lectin overlay demonstrated binding to a single lipid. This interaction was dependent on the presence of calcium and was inhibited by competing saccharides. By assaying column fractions for the ability to bind radioiodinated SP-D after TLC, the glycolipid was purified to homogeneity and identified as phosphatidylinositol (PI). Identification was confirmed by mass spectrometry. We further demonstrate the ability of radiolabeled SP-D to bind to PI presented in a lipid bilayer through separation of free SP-D from liposome-bound SP-D on density gradients of Percoll. The interaction of SP-D with PI is dependent on calcium and inhibited by competing saccharides. SP-D binds with similar efficiency to liposomes with mole fractions of PI ranging from 2.5% to 30%, thereby demonstrating the lectin's ability to recognize mole fractions of PI available in surfactant.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:The major glycolipid recognized by SP-D in surfactant is phosphatidylinositol. 145 14

The terms glycoprotein IV (GPIV) and glycoprotein IIIb (GPIIIb) have been used interchangeably and reports in the literature have indicated this glycoprotein as having a molecular weight variously described as either 88,000 or 97,000, a fast anodal mobility on crossed electrophoresis and either 13 or less than 1 methionine residues on amino acid analysis of the purified glycoprotein. To resolve these discrepancies, we have evaluated the characteristics of GPIV both in whole platelets and after isolation. These studies have shown that the term GPIV defines a protease-resistant platelet surface glycoprotein with Mr 88,330 +/- 2,240 which is immunologically identical with the CD36 differentiation antigen, which migrates with a relatively slow anodal mobility on crossed immunoelectrophoresis and which contains approximately 13 methionine residues per mole.
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PMID:A resolution of reported discrepancies in the characteristics of platelet glycoproteins IV (GPIV) and IIIb (GPIIIb). 169 40

Serum SP1 (pregnancy specific beta 1 glycoprotein), hPL (human placental lactogen) and beta-hCG (beta-human chorionic gonadotropin) in patients with choriocarcinoma, invasive mole, and hydati-diform mole were determined by radioimmunoassay (RIA), and compared with those in normal males, non-pregnant women and normal pregnant women in order to evaluate the clinical significance of SP1, hPL and beta-hCG determinations. Serum SP1 levels at the time of admission were highest in hydatidiform mole (5.1 +/- 0.6 micrograms/L) and lowest in choriocarcinoma (0.5 +/- 0.3 micrograms/L). Serum hPL levels were 68.2 +/- 9.7 ng/L in hydatidiform mole and 26.4 +/- 8.3 ng/L in choriocarcinoma. Serum SP1 and hPL levels in trophoblastic diseases were lower than in normal pregnancies (SP1 11.5 +/- 5.1 micrograms/L, hPL 216.8 +/- 48.1 ng/L). SP1/beta-hCG ratios were less than 1.5 in 4/43 (9.3%) cases of hydatidiform mole and 17/19 (89.5%) cases of invasive mole and choriocarcinoma. The beta-hCG/hPL ratios were below 15 in 35/43 (81.4%) cases of hydatidiform mole and 4/19 (21.1%) malignant trophoblastic diseases. The prognosis after operation and chemotherapy was favourable if patient's SP1 and beta-hCG levels gradually decreased.
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PMID:Serum SP1, hPL and beta-hCG levels in trophoblastic diseases. 172 74


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