Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0268318 (ICP)
 10,007 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effect of changing the amount of external added Co(trp)n and pH values on the interaction of Cu2Zn2 SOD with organic metal compound (Cobalt(II)-Tryptophane) have been studied by means of ICP, VIS and measurement of enzyme activity. It has found that in aqueous solution, there exists a direct interaction of the metal ions of the active center in the metalloenzyme (Cu2Zn2 SOD) with external added Co(Trp)n. As a result, part of the metal ions in metalloenzyme were replaced and the corresponding metalloenzyme derivatives (Co(II)-substituted derivatives of SOD) were produced and the catalytic activity of enzyme were affected. It has also studied the intensity of interactions in different molar ratios (Cobalt(II)-Tryptophane) and pH values and got some results under the effect of corresponding factors.
 ...
PMID:[Study on the interaction of copper-zinc superoxide dismutase with cobalt(II)-tryptophane by spectral analysis]. 1295 39

The role of hemoglobin (Hb) in transmitting the vasodilatory property of NO throughout the vascular system is of much current interest. NO exchange between Hb and low-molecular-weight nitrosothiols such as S-nitrosoglutathione (GSNO) has been speculated and reported in vitro. Previously, we reported that NO delivery from GSNO to Cysbeta93 of human oxyHb is prevented in the presence of the Cu chelators, neocuproine, and DTPA.(1) In the present work, 5 mM solutions of commercial human Hb were found by ICP-MS to contain approximately 20 microM Cu and Zn, suggesting the presence of Cu,Zn-superoxide dismutase (CuZnSOD), which was confirmed by Western blotting. SOD activity measurements were consistent with the presence of approximately 20 microM CuZnSOD monomer in 5 mM Hb solutions, which is the physiological concentrations of these proteins in the red blood cell. Incubation of 3.75 mM oxyHb (15 mM heme; 7.5 mM Cysbeta93) with 3.75 or 7.5 mM GSNO gave rise to 50% or 100% S-nitrosation, respectively, of Cysbeta93 as monitored by FTIR nu(SH) absorption, whereas excess GSNO over Cysbeta93 converted oxyHb to metHb due to the reaction, oxyHb + NO<==>metHb + NO(3)(-). Removal of CuZnSOD by anion-exchange chromatography yielded an oxyHb sample that was unreactive toward GSNO, and replacement with bovine CuZnSOD restored reactivity. Addition of 1 microM GSNO (Cysbeta93/GSNO = 1) to solutions diluted 10(4)-fold from physiological concentrations of oxyHb and CuZnSOD resulted largely in metHb formation. Thus, this work reports the following key findings: CuZnSOD is an efficient catalyst of NO transfer between GSNO and Cysbeta93 of oxyHb; metHb is not detected in oxyHb/GSNO incubates containing close to the physiological concentration (5 mM) of Hb and CuZnSOD when the Cysbeta93/GSNO molar ratio is 0.5 to 1.0, but metHb is detected when the total Hb concentration is low micromolar. These results suggest that erythrocyte CuZnSOD may play a critical role in preserving the biological activity of NO by targeting it from GSNO to Cysbeta93 of oxyHb rather than to its oxyheme.
 ...
PMID:Superoxide dismutase targets NO from GSNO to Cysbeta93 of oxyhemoglobin in concentrated but not dilute solutions of the protein. 1462 85

The effect of changing the amount of external added Co(His)n and phosphate on the interaction of Cu2Zn2SOD with organic metal compound (Cobalt (II)-Histidine) have been studied by means of ICP, VIS and measurement of enzyme activity. It has found that in aqueous solution, there exists a direct interaction of the metal ions of the active center in the metalloenzyme (Cu2Zn2SOD) with external added Co(His)n. As a result, part of the metal ions in metalloenzyme were replaced and the corresponding metalloenzyme derivatives (Co (II)-substituted derivatives of SOD) were produced and the catalytic activity of enzyme were affected. It has also studied the intensity of interactions in different molar ratios (Cobalt (II)-Histidine) and of the presence of phosphate and got some results under the effect of corresponding factors.
 ...
PMID:[Study on the interaction of copper-zinc superoxide dismutase with cobalt (II)-histidine by spectral analysis--II. Effect of amount of external added Co(His)n, phosphate]. 1582 1

The forensic investigator is frequently confronted with the discrimination and deduction of injury implements, which is one of the most important physical testimonies in courts. The usual method used in actual cases is from points of morphology. In the forensic discrimination of injury implements, such as metal implements, the analysis and comparison of elements are expected to provide excellent results, and simultaneous multi-elemental analysis is required to analyze various kinds of elements. This study was designed to establish discrimination and deduction of metal injury implements by scanning electron microscope/energy disperse X-ray microanalyzer (SEM/EDX) and inductively coupled plasma atomic emission spectrometry (ICP-AES). Examined metal particles in five wounds made on the skin of domestic pigs, respectively, using Cu-Zn or Cr-Ni coated and carbon steel kitchen implements by EDX. For carbon steel kitchen implements, analyzed five samples from the back and blade separately in the contents and varieties of elements by ICP-AES. In the wounds by the coated implements, the special particles only containing Cu, Zn or Cr, Ni were found. In the wounds by carbon steel kitchen implements, the particles containing Fe, Cr, Si or Fe, Mn, Si were found. The differences of contents of elements between the back and blade was no significant except No. 5 for carbon steel kitchen implements, and the significant differences of elements exited in Cr, Mn, Si, Cu, Mo among the stainless kitchen knives, Mn, Si among the other kitchen implements and for the blade of No. 5 knife, relative standard deviations (R.S.D.s) were significantly different in Mn, Si, Mo, Ti, S, P, Ni. Using EDX to examine the particles in wounds can deduce the categories of metal injury implements, and we can still deduce the different implements in the same category by ICP-AES.
 ...
PMID:Identify the injury implements by SEM/EDX and ICP-AES. 1662 84

In addition to its superoxide dismutase (SOD) activity, Cu,Zn-superoxide dismutase (CuZnSOD) catalyzes the reductive decomposition of S-nitroso-L-glutathione (GSNO) in the presence of thiols such as L-glutathione (GSH). The GSNO-reductase activity but not the superoxide dismutase (SOD) activity of CuZnSOD is inhibited by the commonly used polyaminocarboxylate metal ion chelators, EDTA and DTPA. The basis for this selective inhibition is systematically investigated here. Incubation with EDTA or DTPA caused a time-dependent decrease in the 680 nm d-d absorption of Cu(II)ZnSOD but no loss in SOD activity or in the level of metal loading of the enzyme as determined by ICP-MS. The chelators also protected the SOD activity against inhibition by the arginine-specific reagent, phenylglyoxal. Measurements of both the time course of SNO absorption decay at 333 nm and oxymyoglobin scavenging of the NO that is released confirmed that the chelators inhibit CuZnSOD catalysis of GSNO reductive decomposition by GSH. The decreased GSNO-reductase activity is correlated with decreased rates of Cu(II)ZnSOD reduction by GSH in the presence of the chelators as monitored spectrophotometrically at 680 nm. The aggregate data suggest binding of the chelators to CuZnSOD, which was detected by isothermal titration calorimetry (ITC). Dissociation constants of 0.08 +/- 0.02 and 8.3 +/- 0.2 microM were calculated from the ITC thermograms for the binding of a single EDTA and DTPA, respectively, to the CuZnSOD homodimer. No association was detected under the same conditions with the metal-free enzyme (EESOD). Thus, EDTA and DTPA must bind to the solvent-exposed active-site copper of one subunit without removing the metal. This induces a conformational change at the second active site that inhibits the GSNO-reductase but not the SOD activity of the enzyme.
 ...
PMID:Binding of polyaminocarboxylate chelators to the active-site copper inhibits the GSNO-reductase activity but not the superoxide dismutase activity of Cu,Zn-superoxide dismutase. 1704 90

Several trace elements, such as Se, Cu, Mn, and Zn are bound to proteins (metallo- and metalloidproteins) in the prostate gland. Currently, it is known that some of those elements play a role in the apoptosis of different cells and redox processes. For the detection of such proteins, analytical and biochemical procedures were combined. SEC and ICP-MS were used to detect some trace elements, which are bound to proteins in the prostate cytosol and/or in the human prostate cell lines. Several antibodies against specific proteins were tested. By means of some of these antibodies several trace element-containing proteins, such as selenoproteins and Cu- and Cu-Zn-proteins, could be identified in the prostate. In addition, the localization of such metal- and metalloid-containing proteins in the micro organelles and cytosol of the prostate indicates specific functions of these proteins because, as it is known, such metal- and metalloid proteins play a role in the apoptosis and especially in the redox processes.
 ...
PMID:Metal-containing proteins in the apoptosis and redox processes in the rat prostate and human prostate cells. 1738 53

A phospholipase A(2) was isolated from the snake venom of Chinese Agkistrodon blomhoffii Ussurensis by column chromatography using DEAE Sephadex A-50 ion-exchange chromatography, Sephadex G-75 gel filtration chromatography and Mono Q ion-exchange chromatography, and designated as Akbu-PLA(2). It showed an average molecular mass of 13,980+/-3 amu determined by MALDI TOF mass spectrometry. Protein identification results from HPLC-nESI-MS/MS analysis indicated that the Akbu-PLA(2) was a new snake venom acidic PLA(2). Seven peptides were sequenced from Akbu-PLA(2) by HPLC-nESI-MS/MS analysis. Sequencing alignment indicated that Akbu-PLA(2) shared homolog peptides of phospholipases A(2) from the venoms of Gloydius ussurensis, Gloydius halys, Gloydius halys (halys viper), Deinagkistrodon acutus and Agkistrodon halys Pallas. Akbu-PLA(2) has an optimum hydrolytic activity temperature of approximately 45 degrees C. The intrinsic fluorescences of Tyr and Trp residues of Akbu-PLA(2) showed emission wavelengths red-shifted by 13.6 and 1.6 nm from those of free Tyr and Trp, respectively. Akbu-PLA(2) was shown to contain one Ca(2+) per monomer by ICP-AES measurement. The Ca(2+) ion was found to be critical for both the hydrolytic activity and the structure of Akbu-PLA(2). Ca(2+) increased the emission fluorescence intensity and the hydrophobicity of the environment of Akbu-PLA(2). The hydrolytic activity of Akbu-PLA(2) was accelerated due to the addition of Ca(2+) ion by enhancing the substrate binding. However, a protein component with the molecular weight two-fold relative to that of Akbu-PLA(2) was found to be difficult to eliminate for the purification of Akbu-PLA(2). HPLC-nESI-MS/MS detected the same peptides from it as from Abku-PLA(2), which indicated that it should be a homodimer of Akbu-PLA(2). A proteomic approach, 2D SDS-PAGE coupled to HPLC-nESI-MS/MS, supported the co-existence of the Akbu-PLA(2) monomer and dimer in the crude snake venom. Results from the combination of phosphoprotein and glycoprotein specific stains combined with the HPLC-nESI-MS/MS method indicated that both the Akbu-PLA(2) monomer and dimer were both phosphorylated and glycosylated. The addition of exogenous Ca(2+) ion was found to be able to promote the dimer formation of Akbu-PLA(2). We conclude that a novel PLA(2) was successfully obtained. The systemically biochemical, proteomic, structural and functional characterization results from Akbu-PLA(2) reveal new threads and provide valuable inputs for the study of snake venom phospholipases A(2).
 ...
PMID:A novel phospholipase A2 from Agkistrodon blomhoffii ussurensis venom: purification, proteomic, functional and structural characterizations. 1927 23

An L-amino acid oxidase (Akbu-LAAO) was isolated from the venom of Agkistrodon blomhoffii ussurensis snake using DEAE Sephadex A-50 ion-exchange, Sephadex G-75 gel filtration, and high performance liquid chromatographies. The homogeneity and molecular mass of Akbu-LAAO were analyzed by SDS-PAGE and MALDI-TOF spectrometry. The sequences of ten peptides from Akbu-LAAO were established by HPLC-nESI-MS/MS analysis. Protein sequence alignment indicated that i) that Akbu-LAAO is a new snake venom LAAO, and ii) Akbu-LAAO shares homology with several LAAOs from the venoms of Calloselasma rhodost, Agkistrodon halys, Daboia russellii siamensis, and Trimeresurus stejnegeri. Akbu-LAAO is a homodimer with a molecular mass of approximately 124.4 kDa. It reacts optimally with its enzymatic substrate, Leu, at pH 4.7 with a K(m) of 2.1 mM. ICP-AES measurements showed that Akbu-LAAO contains four Zn(2+) per dimer that are unessential for the hydrolytic activity of the enzyme. The emission fluorescence intensity of Akbu-LAAO decreases by 61% on removal of Zn(2+) indicating that the zinc probably helps maintain the structural integrity of the enzyme. The addition of exogenous metal ions, including Mg(2+), Mn(2+), Ca(2+), Ce(3+), Nd(3+), Co(2+) and Tb(3+), increases the l-Leu hydrolytic activity of the enzyme. Akbu-LAAO shows apparent anti-aggregation effects on human and rabbit platelets. It exhibits a strong bacteriostasis effect on Staphylococcus aureus, eighteen fold that of cephalosporin C under the same conditions. Taken together, the biochemical, proteomic, structural and functional characterizations reveal that Akbu-LAAO is a novel LAAO with promise for biotechnological and medical applications.
 ...
PMID:Biochemical, functional and structural characterization of Akbu-LAAO: a novel snake venom L-amino acid oxidase from Agkistrodon blomhoffii ussurensis. 2010 May 38

Some experiments to study the influence of electrophoresis conditions and subsequent LA-ICP-MS (laser ablation-inductively coupled plasma mass spectrometry) determination of two metal-binding proteins with different metal-protein affinities (superoxide dismutase, containing Cu and Zn, and alcohol dehydrogenase, containing Zn) are performed. In metal-binding proteins with weak metal-protein affinities, metal losses can happen during electrophoretic separation. It has been demonstrated that the detection of these metals bound to the proteins depends, not only on the nature of the electrophoretic process (naturing or non-denaturing) and post-separation gel treatment, but also on the trailing ion chosen and current applied in the electrophoretic method used. Non-denaturing methods are preferred to denaturing ones in the case of alcohol dehydrogenase being BN-PAGE (Blue Native-Polyacrylamide Gel Electrophoresis) with the use of Tricine as trailing ion the most recommended method. The concentration obtained for Zn in ADH applying BN-PAGE-LA-ICP-MS was 2.6+/-0.30 mg g(-1) very close to the one obtained for ADH solution by ICP-MS (3+/-0.23 mg g(1)). For superoxide dismutase either denaturing or non-denaturing electrophoresis conditions can be used, but a denaturing method based on the use of Tricine as trailing ion is recommended to preserve metals-protein binding when the use of non-denaturing conditions must be avoided. The found concentration for Cu and Zn in SOD after applying SDS-Tris-Tricine-PAGE-LA-ICP-MS was 2.5+/-0.33 and 2.4+/-0.37 mg g(-1) respectively, more or less close (especially for Cu) to the one obtained in SOD solution by ICP-MS (3+/-0.21 and 3.7+/-0.32 mg g(-1) for Cu and Zn). We observe that as higher current is applied the possibility of metal-protein binding losses is higher. In all cases staining of the gel prior to LA-ICP-MS is not recommended.
 ...
PMID:Metal-protein binding losses in proteomic studies by PAGE-LA-ICP-MS. 2018 15

Here we report for the first time the use of species-specific isotope dilution mass spectrometry for the absolute quantification of a metalloprotein using nondenaturing gel electrophoresis laser ablation inductively coupled plasma mass spectrometry (GE-LA-ICP-MS). The concept utilises the intrinsic metals of the metalloprotein for labelling of the isotopically labelled spike ((65)Cu, (68)Zn SOD). The stability of the metal-protein complex under non-denaturing conditions during 1-D PAGE was confirmed and the performance of the method evaluated. Between 4 and 64 microg, SOD was quantified with a recovery rate between 82% and 110% in a standard. The use of the isotopically enriched SOD was utilised to identify the extent of orthogonal diffusion in 1-D gel electrophoresis. Orthogonal diffusion of natural and isotopically enriched SOD in the gel can interfere with the correct determination of the isotope ratios. The matrix effect of a cytosolic liver extract on the non-covalently bound copper and zinc in SOD was evaluated and no significant metal loss from the SOD spike was observed. This study represents the first step necessary for establishing and evaluating the use of a species-specific isotope dilution approach for the absolute quantification of SOD in real samples based on the combination of gel electrophoresis and LA-ICP-MS.
 ...
PMID:Absolute quantification of superoxide dismutase (SOD) using species-specific isotope dilution analysis. 2039 40


1 2 3 4 Next >>