Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A human macrophage colony-stimulating factor encoded by a 4-kilobase cDNA was expressed with bovine papillomavirus vectors in mouse cells. Pulse-chase analyses revealed that the 62-kilodalton (kDa) translation product was glycosylated, cleaved, and efficiently secreted within 1 h of synthesis. The secreted product contained both N-linked and O-linked oligosaccharide chains. Macrophage colony-stimulating factor was present extracellularly as an 80-kDa homodimer and as a multimeric species of greater than 200 kDa that may be associated with other glycoproteins.
Mol Cell Biol 1988 Nov
PMID:Expression and processing of a recombinant human macrophage colony-stimulating factor in mouse cells. 326 78

A growth factor in bovine colostrum was purified to homogeneity by a combination of acid extraction, boiling, cation exchange chromatography, isoelectric focusing, and reverse phase HPLC. The bovine colostrum growth factor (BCGF) had an isoelectric point of about 10, a native mol wt of about 30,000, was resistant to inactivation by boiling and exposure to pH 1, but was inactivated by dithiothreitol. BCGF appeared to be structurally related to human platelet-derived growth factor (PDGF) and competed with human PDGF in a radioreceptor assay. However, while human PDGF appeared to be a heterodimer of 17,000 and 14,000 mol wt subunits, BCGF appeared to be a homodimer of 20,000 mol wt subunits. Purified BCGF had a specific activity in stimulating 3T3 cell proliferation of about 3-6 U/ng and was active at about 1-2 ng/ml.
Mol Endocrinol 1987 May
PMID:Purification and characterization of a bovine colostrum-derived growth factor. 327 92

This study describes the effect of oxygen radicals on the ultrastructure of the isolated Langendorff-perfused rat heart. Oxygen radicals were enzymatically generated by xanthine oxidase (0.025 U/ml) and hypoxanthine (0.96 mM). Hearts were perfusion-fixed for electron microscopy and stereological technique was performed to obtain estimates of volume fractions (Vv) of different tissue components. Perfusion with oxygen radicals resulted in areas with severely damaged myocardial cells. These changes included swelling and cristolysis of mitochondria, disruption of filaments, development of intracellular edema and focal disruption of the sarcolemma. Stereological examination revealed few alterations after 5 min perfusion with oxygen radicals. After 10 min perfusion with oxygen radicals, however, the Vv (myocyte/myocardium) increased from 0.542 +/- 0.042 (mean +/- S.D.) to 0.663 +/- 0.144, and this paralleled the development of Vv (cellular edema/myocyte) being 0.047 +/- 0.028. Vv (capillary wall/capillary) increased from 0.215 +/- 0.046 to 0.411 +/- 0.123 indicating endothelial swelling. Although the mitochondria appeared swollen, Vv (mitochondria/myocyte) remained constant. The effect of a 35 min recovery period on the ultrastructure was minor. The application of SOD and catalase together with xanthine oxidase and hypoxanthine reduced the observed changes significantly, thus proving the participation of oxygen radicals. This study confirms that oxygen radicals can induce major alterations in myocardial ultrastructure.
J Mol Cell Cardiol 1987 Apr
PMID:Ultrastructural changes induced in the isolated rat heart by enzymatically generated oxygen radicals. 361 20

Addition of vanadate, stimulated oxidation of NADH by rat liver microsomes. The products were NAD+ and H2O2. High rates of this reaction were obtained in the presence of phosphate buffer and at low pH values. The yellow-orange colored polymeric form of vanadate appears to be the active species and both ortho- and meta-vanadate gave poor activities even at mM concentrations. The activity as measured by oxygen uptake was inhibited by cyanide, EDTA, mannitol, histidine, ascorbate, noradrenaline, adriamycin, cytochrome c, Mn2+, superoxide dismutase, horseradish peroxidase and catalase. Mitochondrial outer membranes possess a similar activity of vanadate-stimulated NADH oxidation. But addition of mitochondria and some of its derivative particles abolished the microsomal activity. In the absence of oxygen, disappearance of NADH measured by decrease in absorbance at 340 nm continued at nearly the same rate since vanadate served as an electron acceptor in the microsomal system. Addition of excess catalase or SOD abolished the oxygen uptake while retaining significant rates of NADH disappearance indicating that the two activities are delinked. A mechanism is proposed wherein oxygen receives the first electron from NAD radical generated by oxidation of NADH by phosphovanadate and the consequent reduced species of vanadate (Viv) gives the second electron to superoxide to reduce it H2O2. This is applicable to all membranes whereas microsomes have the additional capability of reducing vanadate.
Mol Cell Biochem 1987 Jun
PMID:Vanadate-stimulated NADH oxidation in microsomes. 365 Jun 94

NADH-dependent reduction of polyvanadate was observed by using rat liver microsomes as the enzyme source. The reduced vanadate form obtained was blue in color with a broad absorption maximum in the red region around 650 nm. Microsomes and phosphate anions were found to be essential for polyvanadate reduction. The rate and the extent of formation of blue color compound was dependent on the amount of vanadate present. Cytochrome b5 was found to be involved in this SOD-insensitive reaction. The rate of disappearance of the blue-colored compound was dependent on concentration of NADH and was found to be sensitive to SOD. Catalase and Mn2+, which inhibit oxygen consumption accompanying NADH oxidation, increased both the rate and extent of the blue color compound formed. The results suggest that vanadate acts as an electron acceptor.
Mol Cell Biochem 1987 Jun
PMID:NADH-dependent polyvanadate reduction by microsomes. 365 Jun 95

The biochemical features of a membrane antigen detected by a mouse monoclonal antibody (A1) raised against the murine thymoma cell line EL4 are described. This reagent detected a novel disulfide-linked 90,000 mol. wt dimeric membrane glycoprotein composed of two chains of approx 45,000 mol. wt. Endo-beta-N-acetylglucosaminidase F digestion generated a single 28,000 polypeptide, thus suggesting that the A1 molecule is a homodimer. No structural homology between the A1 molecule and the human T 90/44 protein (9.3 antigen) could be revealed by peptide mapping analysis. In view of the fact that three polypeptides of mol. wts 28,000-30,000, 21,000 and 15,000 respectively co-precipitated with the A1 antigen, the possible relationship of the A1 molecular complex to other known T-cell surface antigens including the antigen receptor is discussed.
Mol Immunol 1987 Jul
PMID:Biochemical characterization of a T-lymphoma-specific 90,000 molecular weight disulfide linked dimeric glycoprotein. 365 4

The chemical nature of the inactivation of citrate synthase by S-(4-bromo-2,3-dioxobutyl)-CoA, an active site-directed irreversible inhibitor, has been investigated. Active site-directed inactivation leads to derivatization of either Lys22 by epsilon-amino Schiff base formation or Glu363 by apparent alkylation of the gamma-carboxyl group, respectively. Lys22 is labeled in the tight (catalytic) form of the enzyme while Glu363 is labeled in the open (product release) form. Glu363 and Lys22 are both located at or near the entrance to an active site in the crystal structure of citrate synthase (Remington, S., Wiegand, G., and Huber, R. (1982) J. Mol. Biol. 158, 111-152). Glu363 is in the sequence of the protomer forming the active site while Lys22 is in the sequence of the other polypeptide in the homodimer. Labeling in this region appears to inactivate the enzyme by preventing access of substrates to the active site. A distinct and separate labeling process involves derivatization of Asn192 in the tight (catalytic) form and Ser198 and/or Ser199 in the open (product release) form at a locus far removed from the active site. Labeling at the second site may simply identify chemically reactive residues, or it may identify the binding site for long chain acyl-CoA, which has been identified as a possible allosteric negative effector of citrate synthase (Caggiano, A. V., and Powell, G. L. (1979) J. Biol. Chem. 254, 2800-2806). This second labeling process apparently inactivates the enzyme by interfering with catalytically essential conformational changes.
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PMID:S-(4-bromo-2,3-dioxobutyl)-CoA labels two distinct sites on citrate synthase. 372 59

Myosin from chicken pectoralis muscle consists of isozymes that differ in their alkali light chains. It is possible to isolate alkali 1 (A1) and alkali 2 (A2) homodimers of native myosin by immunoadsorption methods, and to compare their steady-state kinetics as well as their assembly into synthetic filaments under a variety of ionic conditions. Bipolar filaments of the isozymes formed at low salt concentrations had a narrow length distribution and did not differ from controls made from unfractionated myosin. Chicken myosin also assembles into highly homogeneous minifilaments similar to those formed by rabbit myosin in a citrate/Tris buffer. Analytical ultracentrifugation and electron microscopy showed that A1-homodimer, A2-homodimer and unfractionated myosin assembled into 0.3 micron short, bipolar minifilaments, which were indistinguishable from one another in size and shape. The steady-state myosin ATPase activity of the two homodimeric isozymes was identical in K+(EDTA) and Ca2+ assay media. The actomyosin Mg2+ ATPase measured at 25 and 55 mM-KCl (pH 8.0) showed only minor differences in both Vmax and Kapp. Actomyosin activity was also determined for the more homogeneous minifilament preparations of the isozymes and these, as well, produced essentially indistinguishable kinetic parameters. Thus we find no evidence to support the hypothesis that a particular alkali light chain of myosin can affect either the structure of the filaments or the steady-state rate of ATP hydrolysis.
J Mol Biol 1983 Oct 25
PMID:Assembly and kinetic properties of myosin light chain isozymes from fast skeletal muscle. 622 5

Messenger RNA is released preferentially from isolated rat liver nuclei in the presence of the ATP-generating system and cytosol. The release is suppressed by spermidine, while cytoplasmic RNase inhibitor was ineffective and PCMB like some other thiol-blocking agents inhibitory. Cytoplasmic SOD added to the system strongly suppressed RNA release. A similar effect could be obtained by anaerobiosis due to addition of SMP. In both cases the inhibition is reversed by cyanide. In contrast to normal liver where the generation of superoxide radicals takes place almost exclusively in microsomes and is coupled with the oxidation of NADPH, in mouse ascites hepatoma 22a the generation of superoxide radicals occurs mainly in the nuclear envelope and is coupled wih the oxidation of both NADPH and NADH and inhibited by cyanide.
Mol Biol Rep 1981 May 22
PMID:Some features of nucleo-cytoplasmic RNA transport from isolated nuclei. 626 58

One of the major forms of glutathione S-transferase (designated as Ft transferase) has been identified and purified to near homogeneity from mouse testis. The purification was achieved by ammonium sulfate fractionation, DEAE cellulose chromatography, hydroxylapatite chromatography and the preparative isoelectric focusing. Purified Ft transferase has an isoelectric point of 4.9 +/- 0.3 and was shown to be a homodimer with a native molecular weight of about 50000. Immunologically, antisera to Ft transferase do not crossreact with F2 or F3 transferase. However, a weak cross reactivity was observed between the antisera to F3 transferase and FT transferase. Biochemical properties of purified Ft transferase are similar to those transferases isolated from mouse liver. Tissue distributions of the multiple forms of glutathione S-transferase were examined by column isoelectric focusing of various mouse tissue homogenates. It was found that mouse Ft transferase is present only in testis as a major form and in brain as a minor form, but not in other tissues that were examined.
Mol Cell Biochem 1982 Dec 10
PMID:Biochemical and immunological analysis of an abundant form of glutathione S-transferase, in mouse testis. 681 53


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