Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0272170 (SDS)
 50,377 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The ba3 quinol oxidase from Paracoccus denitrificans has been purified by a new protocol leading to significantly higher yields than previously reported (Richter et al. (1994) J. Biol. Chem. 269, 23079-23086). In an SDS PAG an additional protein band compared with the previous preparation appears, which can be identified as the major form of subunit II. All protein bands can be assigned to genes of the qox operon by N-terminal sequencing, indicating that the oxidase consists of four subunits. In addition to one heme A, one heme B, and one copper atom, the preparation contains two ubiquinone molecules per enzyme. The oxidase is further characterized by electron paramagnetic resonance (EPR), circular dichroism (CD) and magnetic circular dichroism (MCD) spectroscopy.
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PMID:Biochemical and spectroscopic properties of the four-subunit quinol oxidase (cytochrome ba3) from Paracoccus denitrificans. 895 Mar 74

Human fibrinogen exposed to 46.5 degrees C was subjected to gel permeation chromatography. The protein eluted in two distinct peaks. The first peak appeared in the void volume containing soluble fibrinogen aggregates, while the other peak represented monomeric fibrinogen. In contrast to the monomeric peak material, the aggregate fraction reacted with a panel of monoclonal antibodies specific for fragment D-dimer using an ELISA system. Edman degradation showed that both the aggregate and the monomeric fractions were devoid of soluble fibrin, and immunoblots of SDS-PAG electrophoretic profiles disclosed no sign of stabilized high molecular weight derivatives. We have previously shown that the aggregate fraction of similarly treated fibrinogen, in contrast to the monomeric fraction, stimulates the t-PA catalyzed conversion of plasminogen to plasmin and concomitantly exposes the sequences Aalpha-(148-160) and gamma-(312-324) involved in t-PA stimulation. Our present and previous findings suggest that soluble fibrinogen aggregates possess a fibrin-like structure, and that fibrin or fibrinogen polymer formation is a prerequisite for the enhancing effect on t-PA-mediated plasminogen to plasmin conversion which is seen even with the polymers in the soluble state.
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PMID:D-dimer specific monoclonal antibodies react with fibrinogen aggregates. 916 70

The fungal strain Humicola lutea 110 produces a mangan- and a copper zinc-containing superoxide dismutases (SOD). In this study, the purification, N-terminal sequence and spectroscopic properties of the new Cu,Zn SOD are described. The preparation of the pure metalloenzyme was achieved via treatment of the strain with acetone followed by gel and ion exchange chromatography. The protein consists of 302 amino acid residues and has a molecular mass of approximately 32 kDa, as determined by PAG electrophoresis and 3100 U mg-1 protein-specific activity. It is a dimeric enzyme with two identical subunits of 15,950 Da, as indicated by SDS-PAGE, mass spectroscopic and amino acid analysis. The N-terminal sequence analysis of the Cu,Zn SOD from the fungal strain revealed a high degree of structural homology with enzymes from other eukaryotic sources. Conformational stability and reversibility of unfolding of the dimeric enzyme were determined by fluorescence and circular dichroism (CD) spectroscopy. The critical temperature of deviation from linearity (Tc) of the Arrhenius plot ln (Q-1(-1)) vs. 1/T was calculated to be 68 degrees C and the respective activation energy for the thermal deactivation of the excited indole chromophores is 42 kcal mol-1. The melting temperatures (Tm) were determined by CD measurements to be 69 degrees C for the holo- and 61 degrees C for the apo-enzyme. The fluorescence emission of the Cu,Zn SOD is dominated by 'buried' tryptophyl chromophores. Removal of the copper-dioxygen system from the active site caused a 4-fold increase of the fluorescence quantum yield and a 10 nm shift of the emission maximum position towards higher wavelength.
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PMID:A novel Cu,Zn superoxide dismutase from the fungal strain Humicola lutea 110: isolation and physico-chemical characterization. 1058 36

Three cytolytic toxins (RTX: RTX-A, RTX-S, and RTX-G) were isolated from the sea anemone Radianthus macrodactylus and characterized. The purification scheme involved hydrophobic chromatography on Polychrom-1, batch-chromatography on CM-23 cellulose, gel filtration on Akrilex P-4, cation-exchange chromatography on CM-32 cellulose, and HPLC on an ion-exchange Ultropac TSK CM-3SW column and a reversed-phase Silasorb C18 column. The molecular masses of RTXs (ca. 20 kDa) were determined by SDS-PAGE in a density gradient of PAG. They are highly basic polypeptides (pI of 9.8 for RTX-A and RTX-S and 10.5 for RTX-G) containing similar amino acid compositions with a high content of basic and hydrophobic residues and the absence of Cys residues. The hemolytic activities of RTX-A, RTX-S, and RTX-G were determined to be 3.5, 5.0, and 1.0 x 10(4) HU/mg, respectively. Exogenous sphingomyelin inhibits their action on the erythrocyte membrane. The N-terminal sequence of RTX-A was determined to be ALAGAIIAGAGL/KGLKI/FLIEVLGEG--V/NKVKI-.
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PMID:[Isolation and characteristics of high molecular weight cytolysins from the sea anemone Radianthus macrodactylus]. 1064 76

Human rhinosporidial tissue was used as the source of the various developmental stages of Rhinosporidium seeberi--endospores with electron dense bodies, juvenile, and immature sporangia. After homogenisation in phosphate buffered saline (PBS) and removal of tissue fragments by centrifugation, the rhinosporidial bodies were isolated on centrifuged Percoll columns with gradients of densities or on triple-layered columns of varying density. The separated bands, after repeated washing in PBS gave bodies free from human tissue as shown on Leishman and PAS staining and indirect immunofluorescence with rabbit and human patients' anti-rhinosporidial sera. Sonicates of these bodies were tested on agarose gel for precipitation with antisera, and on SDS-PAG electrophoresis and Coomassie Blue staining. Percoll columns were shown to be capable of isolating these stages of R. seeberi, free from human tissue and contaminating bacteria.
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PMID:Purification of the endospores and sporangia of Rhinosporidium seeberi on Percoll columns. 1068 45

The work focused on the penultimate enzyme, prothrombin, in the coagulation cascade. Prothrombin was purified and characterized from ostrich plasma. The results obtained contribute to a better understanding of blood coagulation in the ostrich and the evolution of prothrombin and the coagulation cascade. Prothrombin was purified from ostrich plasma by barium chloride precipitation, ammonium sulfate fractionation, and DEAE-cellulose and Cu(2+)-chelate Sepharose chromatography. Ostrich prothrombin exhibited a M(r) of 72,800 and a pI of 6.9 using SDS-PAGE and PAG-isoelectrofocusing, respectively. The N-terminal sequence of ostrich prothrombin showed 78 and 87% identity with human and bovine, respectively. The cDNA was isolated from ostrich liver and the predicted amino acid sequence compared with those from other species. Ostrich prothrombin shares sequence identity with chicken (84%), human (60%), bovine (59%), rat (60%), mouse (59%) and hagfish (50%) prothrombin, suggesting a common function of prothrombin in these vertebrates. Amino acid sequence identities indicate that the thrombin beta-chain (62%) and the propeptide-Gla (75%) domains are the regions most constrained for the common functions of vertebrate prothrombins. Ostrich prothrombin, therefore, shows similarity in structure to other vertebrate prothrombins.
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PMID:Purification and characterization of ostrich prothrombin. 1113 55

In the present work, two biochemical approaches were used to characterize PAGs isolated from Bos indicus fetal cotyledons removed at different gestational ages. The first procedure included acidic and ammonium sulfate precipitations, anion and cation exchange chromatographies and the second included pepstatin-agarose affinity chromatography. A bovine PAG radioimmunoassay was used to monitor the immunoreactivity throughout the isolation procedures. The most immunoreactive fractions issued from cation exchange and affinity chromatographies were analyzed by SDS-PAGE and Western blotting, before transfer to a polyvinylidene difluoride (PVDF) membrane for NH2-microsequence determination. Use SDS-PAGE and Western blotting, different isoforms of PAG with apparent molecular masses of 51 to 69 kDa and isoelectric points varying from 4.4 to 6.7 were identified in the placentas from different gestational ages. N-terminal microsequencing (10 to 25 aa long) indicates the expression of one single terminal amino acid sequence in the Bos indicus placenta, which is 100% identical to the bovine PAG-1.
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PMID:Characterization of pregnancy-associated glycoproteins extracted from zebu (Bos indicus) placentas removed at different gestational periods. 1240 51

AMP-deaminase (EC 3.5.4.6) is a key enzyme of nucleotide breakdown involved in regulation of adenine nucleotide pool in the liver. Mechanisms regulating activity of the enzyme are not completely elucidated, till now. In this paper experimental data indicating on the potential regulatory significance of changes in oligomeric structure of the enzyme are presented. SDS-PAG electrophoresis of human liver AMP-deaminase revealed the presence of three enzyme fragments. Only largest of them (the protein fragments weighing 68 kDa) reacted immunologically with anti- (human liver) AMP-deaminase antibodies. At physiological pH 7.0, in the absence of regulatory ligands, reaction catalysed by human liver AMP-deaminase was strongly dependent on enzyme concentration used, with half-saturation constant (S0.5) values increasing significantly with the degree of enzyme dilution. Preincubation with activated long-chain fatty acids--substances promoting dissociation of oligomeric enzymes, inhibited the activity of AMP-deaminase studied nearly completely. Gel filtration on Sepharose CL-6B column demonstrated existence of at least three active oligomeric forms of human liver AMP-deaminase. We postulate that oligomeric structure of the enzyme is a factor determining regulatory profile of AMP-deaminase studied.
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PMID:Human liver AMP-deaminase--oligomeric forms of the enzyme. 1248 28

Bacillus subtilis BS-98 is one of the antagonistic strains strongly against plant fungal pathogens such as Physalospora piricola Nose. The antifungal protein was purified by ammonium sulphate precipitation and column chromatography on Sephadex G-100 and DEAE-cellulose, and it was named X98III. Molecular weight of X98III is 59,000 by SDS-PAGE and PI value is 4.50 by PAG-IEF, respectively. X98III was demonstrated as glycoprotein and lipoprotein by CAM (cellulose acetate membrane) electrophoresis and special staining. We estimated it contains 6% saccharides by using DNS methods. This protein was also found to be thermostabale and partially sensitive to proteinases. The amino acid analysis of the protein X98III showed that it comprises of 11 different amino acids and Glu, Tyr, Cys are the abundant amino acids. No Asp, Phe and Met were found. Purified X98III has strong inhibiting activity against the pathogens of Physalospora piricola, Phoma asparagi, etc. The antifungal mechanism of X98III was mainly disintegration of the cell wall to make the hyphae abnormal and the spores germinate abnormally or can not germinate at all.
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PMID:[Purification and properties of antifungal protein X98III from Bacillus subtilis]. 1254 83

The study aimed at determination of circulating immune complexes (CIC) levels in a serum of patients with ischemic and hemorrhagic strokes, isolation of the complexes and their antigen composition identification. Spectrophotometric assay, polyethylene glycol precipitation and SDS PAG electrophoresis were used. Comparing to controls, significantly elevated levels of both small and big CIC were detected in the serum of the patients with ischemic stroke, while in the patients with hemorrhage stroke only the level of small CIC was elevated. The antigen CIC composition was specific for each stroke form and for control group either. Being compared to literature data, the results obtained revealed a specificity of the antigen CIC composition in ischemic and hemorrhagic strokes.
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PMID:[Circulating immune complexes in ischemic and hemorrhagic strokes]. 1283 May 18


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