Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.16.3.1 (ceruloplasmin)
5,074 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Membrane receptors for ceruloplasmin were isolated by affinity chromatography using CP bound to CNBr-activated Sepharose 4B. The receptor was obtained in the form of a single sharp peak which when collected, concentrated and run on SDS-PAGE provided a single band with a molecular weight of 35,000. Treatment with endoglycosidase F reduced this molecular weight by 3%. It is concluded that ceruloplasmin receptors in this cell system is a membrane protein containing 3% carbohydrate with a total molecular weight of 35,000. It is possible that this is a monomer of a higher molecular weight protein.
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PMID:Purification and characterization of ceruloplasmin receptors. 256 40

The ability of major serum proteins (albumin, immunoglobulin G) and free radical scavenger proteins (ceruloplasmin, superoxide dismutase, transferrin) to interact with O2-. and OCl- was studied. The interaction between serum proteins and OCl- was shown to be nonspecific and cause protein degradation. During SDS polyacrylamide gel electrophoresis ceruloplasmin and transferrin were degraded in the highest degree. Protein damage was also recorded by fluorescence changes. It is suggested that the damaging influence of active oxygen species secreted by stimulated neutrophils into the extracellular space can be abolished only by ceruloplasmin.
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PMID:[Antioxidative properties and degradation of serum proteins by active oxygen forms (O2-., OCl-) generated by stimulated neutrophils]. 284 8

Ceruloplasmin is a blue copper-containing serum glycoprotein with oxidase activity. It as been proposed that the physiological function of ceruloplasmin involves the oxidation of ferrous iron and its incorporation into apotransferrin. There are several reports demonstrating that ceruloplasmin is made up of multiple chains. Ryden has questioned the multichain structure of ceruloplasmin from human, pig, horse and rabbit sera, arguing that the dissociation observed by previous workers could be attributed to cleavage of labile bands in the protein by enzymatic contaminants present in commercial preparations of the protein. By introducing epsilon-aminocaproic acid, a general protease inhibitor, at the beginning of the enzyme preparation, Ryden proposed a single-chain structure for ceruloplasmin. On the contrary the results presented by Freeman and Daniel showed that human ceruloplasmin is a multichain protein. In this paper we report a new purification method for horse ceruloplasmin which furnishes a homogeneous protein preparation in high yield and with good reproducibility. This procedure allowed to determine with greater accuracy the molecular mass of the protein, of 120,000 daltons by gel chromatography and 115,000 daltons by SDS gel electrophoresis. The protein is composed of one unit only and contains 6 copper atoms. Horse ceruloplasmin is a glycoprotein containing about 20% carbohydrate by weight.
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PMID:Horse plasma ceruloplasmin molecular weight and subunit analysis. 343 54

Following intravenous administration to rats of the azo dye hepatocarcinogen 3'-methyl-N,N-dimethyl-4-aminoazo-[14C]benzene, 60-70% of the injected dose was recovered in bile in 2 h. Approximately 10% of bile radioactivity was trichloroacetic acid-precipitable, not extracted by n-butanol and non-dialyzable. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of bile followed by fluorography revealed two major and several minor proteins to which radiolabelled azo dye metabolites were bound; one of these major proteins (50 kDa) was purified from bile and shown to be homogeneous by SDS-polyacrylamide gel electrophoresis, isoelectric focusing (pI 7) under denaturing conditions and N-terminal analysis. The protein (MBP) comprises 15% of the total bile protein. Amino acid analysis revealed a preponderance of acidic and hydrophobic amino acids. The absorption spectrum of the native protein had a major peak at 280 nm and minor peaks at 345, 400, 600 and 650 nm. The fluorescence spectrum showed a major excitation maxima at 285 and 350 nm and corresponding emission maxima at 345 and 440 nm. Atomic absorption spectroscopy revealed 5 atoms of Cu per mol protein. Approximately 90% of the Cu was EPR silent. MBP did not react with antisera directed against rat serum IgA, albumin or ceruloplasmin; nor did these proteins react against antisera to MBP. Seven distinct peptide bands ranging from 5 to 18 kDa were obtained when MBP was subjected to CNBr cleavage and the digests were analyzed by SDS-polyacrylamide gel electrophoresis. The [14C]-Me-DAB derived radioactivity was present in only two of the peptides, indicating specific binding sites for azodye metabolites.
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PMID:Purification and characterization of a novel abundant protein in rat bile that binds azo dye metabolites and copper. 630 47

From rat livers labeled in vivo for 30 min with [35S] cys-met, we have isolated two classes of vesicular carriers operating between the Golgi complex and the basolateral (sinusoidal) plasmalemma. The starting preparation is a Golgi light fraction (GLF) isolated by flotation in a discontinuous sucrose density gradient and processed through immunoisolation on magnetic beads coated with an antibody against the last 11 aa. of the pIgA-R tail. GLF and the ensuing subfractions (bound vs nonbound) were lysed, and the lysates processed through immunoprecipitation with anti-pIgA-R and anti-albumin antibodies followed by radioactivity counting, SDS-PAGE, and fluorography. The recovery of newly synthesized pIgA-R was > 90% and the distribution was 90% vs 10% in the bound vs nonbound subfractions, respectively. Albumin radioactivity was recovered to approximately 80%, with 20% and 80% in bound vs nonbound subfractions, respectively. Other proteins studied were: (a) secretory-apolipoprotein-B, prothrombin, C3 component of the complement, and caeruloplasmin; (b) membrane-transferrin receptor, EGR-receptor, asialoglycoprotein receptor, and the glucose transporter. In all the experiments we have performed, the secretory proteins distributed up to 85% in the nonbound subfraction (large secretory vacuoles), whereas the membrane proteins were segregated up to 95% in the bound subfraction (small vesicular carriers). These results suggest that in hepatocytes, membrane and secretory proteins are transported from the Golgi to the basolateral plasmalemma by separate vesicular carriers as in glandular cells capable of constitutive and regulated secretion.
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PMID:Membrane and secretory proteins are transported from the Golgi complex to the sinusoidal plasmalemma of hepatocytes by distinct vesicular carriers. 818 43

Long-Evans Cinnamon(LEC) mutant rats exhibited less than 5% of normal levels of serum ceruloplasmin oxidase activity, but immunoblot analysis showed normal levels of immunologically detectable ceruloplasmin protein in sera from the mutant rats. Immunostaining of cryosections from the liver tissues with anti-ceruloplasmin antibody showed no significant difference between normal and LEC rats. Results from pulse labeling of ceruloplasmin for 3 hours with [35S]methionine in primary hepatocyte culture, followed by immunoprecipitation, SDS-PAGE and fluorography, showed only minor changes in ceruloplasmin protein synthesis and secretion. These results suggest that the mutation(s) does not affect ceruloplasmin gene expression, but results in a failure in the mechanism whereby copper is incorporated into newly synthesized apoceruloplasmin to produce oxidase active holoform.
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PMID:Deficiency of holo-, but not apo-, ceruloplasmin in genetically copper-intoxicated LEC mutant rat. 823 29

Ceruloplasmin, a copper carrier protein in mammal serum, was isolated by a variation of the Neo-Zgirski method consisting of a chromatography column in DEAE Sephadex A-50 gel, using different buffers for its selective elution. This protein was then precipitated with ammonium sulfate and an ethanol chloroform mixture. Finally, a dialysis against sodium acetate was performed and the samples were purified. In addition, the protein concentration and its characterization were determined. Enzyme kinetics were calculated using paraphenylenediamine as an artificial substrate, determined by the Michaelis constant. Furthermore, an SDS electrophoresis in polyacrylamide gel was performed, and the samples of porcine ceruloplasmin were compared with commercial bovine ceruloplasmin. Finally, a comparative study was carried out between the ceruloplasmin levels in serum from patients with chronic renal insufficiency (CRI) undergoing hemodialysis treatment in artificial kidneys with a cuprophan membrane, with a control group of donors. A similar study was performed with a group of patients suffering from the same illness, but undergoing dialysis treatment with polyacrylonitrile membrane. These results were expressed in mg% in relation to the ceruloplasmin isolated previously.
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PMID:Study of ceruloplasmin in renal insufficiency. 833 18

Ferritin was purified from the hepatopancreas of the freshwater crayfish Pacifastacus leniusculus after injection of iron. It has the same size as horse spleen ferritin (440 kDa) and migrates as two bands, 19 kDa and 20 kDa, respectively, in SDS/PAGE under reducing conditions. Crayfish ferritin (20 kDa) was cloned from a hepatopancreas cDNA library. The deduced amino acid sequence of the crayfish ferritin shows a closer relationship to vertebrate ferritin heavy chains than to insect ferritin and contains the conserved H-specific residues for the ferroxidase centre found in vertebrate ferritin heavy chain. An IRE(iron-responsive element)-like sequence with a predicted stem-loop structure was present in the 5' untranslated region of the crayfish ferritin mRNA. Crayfish ferritin does not share the atypical properties of insect ferritins, such as high molecular mass of intact protein, abundance in hemolymph, and export into vacuoles. We suggest that there are two different types of ferritins distributed in different species: insect-type or secretory ferritins which are predominant in the snail oocyte and insects, and vertebrate (crustacean)-type or cytosolic ferritins which are predominant in vertebrates and crustacea.
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PMID:Purification and cDNA cloning of ferritin from the hepatopancreas of the freshwater crayfish Pacifastacus leniusculus. 861 15

Previous studies have suggested that copper is incompletely incorporated into caeruloplasmin, the major plasma form of copper-transporting protein, in the genetic copper toxic condition, Wilson's disease. In this paper we have investigated the role of copper and caeruloplasmin in the abnormal biliary copper transport and characterizes Wilson's disease. Using SDS/PAGE and Western blotting, we have demonstrated the presence of holocaeruloplasmin in liver samples from patients with Wilson's disease (abnormal biliary copper excretion) and in control patients (normal biliary copper excretion). The presence of holocaeruloplasmin was also confirmed by measurement of caeruloplasmin oxidase activity using staining with o'Dianisidine. In contrast with the findings in liver tissue, holocaeruloplasmin was absent from bile from patients with Wilson's disease, but as expected it was present in the bile from control subjects. We have also identified and partially characterized a 189-200 kDa protein from purified human biliary canalicular membranes which binds copper and possesses caeruloplasmin-like activity when probed with a specific human anti-caeruloplasmin antibody. In conclusion, we have demonstrated that copper incorporation in caeruloplasmin is normal in patients with Wilson's disease contrary to previous reports. Secondly, we have shown that the defect in Wilson's disease appears to lie in the biliary canalicular excretion of holocaeruloplasmin resulting in its retention within the hepatocyte causing copper toxicosis. Finally we have identified and partially characterized a caeruloplasmin-binding protein from biliary canalicular membranes which may provide a link to the gene defect in Wilson's disease.
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PMID:New insights into the pathogenesis of copper toxicosis in Wilson's disease: evidence for copper incorporation and defective canalicular transport of caeruloplasmin. 864 67

A protein reacting with a monoclonal antibody against human placental diamine oxidase was purified from the specific granules of human neutrofil granulocytes using affinity chromatography on aminohexyl-divinylsulfonyl-agarose. The protein had an M(r) determined by SDS/PAGE, corresponding to diamine oxidase, but had other properties which indicated that it might be a different protein. A combination of protein chemical techniques, including N-terminal sequencing, identified the protein as lactoferrin, an iron-containing protein with an M(r) of approximately 800000, a high isoelectric point and ferroxidase activity. Purified commercial lactoferrin was shown to bind to aminohexyl-divinylsulfonyl-agarose, and to be eluted in a heterogenous way from the matrix by amines and salt. Alignment of the sequences of diamine oxidase and lactoferrin showed that they are similar, indicating a common ancestry for these two different classes of metallo-oxidases.
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PMID:Lactoferrin: similarity to diamine oxidase and purification by aminohexyl affinity chromatography. 889 21


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