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)

Whole blood, plasma, or serum levels of various components were measured in fasting, drug-free control subjects and drug-free schizophrenic patients. Compared to normal controls, chronic schizophrenic patients showed increased alpha2-globulins and decreased plasma cholinesterase activity and ceruloplasmin activity, and acute schizophrenic patients showed decreased alpha2-globulins. Compared to chronic patients, acute schizophrenics showed decreased alpha2-globulins and IgA. Compared to normal controls of similar age, chronic schizophrenic patients weighed less, were shorter, and had smaller body surface area. The acute schizophrenic patients were significantly younger than the normal subjects or chronic schizophrenics but there was no difference in the other physical measurements. The present study indicates no gross disturbances in the blood variables studied. That some differences are statistically significant from controls is of scientific interest, but of no clinical value in the diagnosis of schizophrenia.
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PMID:Blood protein fraction comparisons of normal and schizophrenic patients. 4 63

A galactose-specific lectin isolated from Ricinus communis beans has been covalently coupled to Sepharose 4B activated with cyanogen bromide. The immobilized lectin retains its polysaccharide-binding property. The Sepharose-lectin can be used for the purification of polysaccharides containing terminal nonreducing galactose. Only a small fraction of 'native fetuin' and 'native ceruloplasmin' are retarded on Sepharose-lectin. On analysis it was observed that they had a lower content of sialic acids as compared to the native and unbound glycoproteins (sialated fractions). However, on desialation, fetuin and ceruloplasmin were completely adsorbed to Sepharose-lectin. The asialoglycoproteins interact strongly with Sepharose-lectin as compared to 'partially sialated glycoproteins'. This has been attributed to the exposure of galactose residues of these glycoproteins on enzymatic desialation. These experiments demonstrated that Sepharose-lectin interacts with glycoproteins through their terminal, non-reducing galactose. On the basis of these experiments it is suggested that Sepharose-lectin can be used as an analytical tool for separation of 'fully sialated glycoproteins' from the 'partially sialated glycoproteins'.
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PMID:Affinity chromatography of galactose containing biopolymers using covalently coupled Ricinus communis lectin to Sepharose 4B. 5 50

In 9 groups of liver diseases, 11 serum protein parameters were studied. Prealbumin, retinol-binding protein, albumin, alpha-lipoprotein and Normotest (NT) were usually highly intercorrelated and separated best among groups with different types of functional impairment. Haptoglobin, C3 and total iron-binding capacity were probably also sometimes reduced by restricted protein synthesis but appeared to be more easily affected by other factors, alpha1-antitrypsin was often increased in different liver diseases, but a pattern compatible with the "acute-phase reaction" was regularly present only in hepatic tumors. Bile retention was often accompanied by relatively high levels of ceruloplasmin, C3, and alpha-lipoprotein and by high NT values.
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PMID:Serum proteins in diseases of the liver. 5 85

The effect of zinc deficiency on protein synthesis in rats during tularemia was studied. Five weeks prior to infection with the live vaccine strain of Francisella tularensis, rats had been assigned to one of three dietary groups: zinc deficient (-Zn), pair-fed (PF) or ad libitum (AL). Within 4 weeks, zinc deficiency manifested itself by diminished growth rate, decreased serum and liver zinc concentrations and alopecia. By 18 hour post infection, rats of all groups were febrile and exhibited an increased hepatic uptake of zinc. Despite initially lower concentrations of seromucoid in the PF and -Zn groups, infection elicited an increase in seromucoid concentration as well as enhanced incorporation of 3H-leucine into this fraction of comparable degree in all dietary groups. The same held true for ceruloplasmin. Alpha 2-macrofetoprotein also increased to the same extent in all dietary groups. Infection was associated with a decrease in extractable albumin in ad libitum and pair fed control groups. Only the -Zn group showed a significant decrease in specific activity suggestive of diminished albumin synthesis. Zinc deficiency of itself did not cause a decrement in radiolabel in muscle protein. Thus, despite documented zinc deficiency, rats subjected to the stress of infection respond by synthesizing increased amounts of acute phase globulins apparently at the expense of serum albumin and muscle protein synthesis.
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PMID:Protein synthesis in zinc deficient rats during tularemia. 5 80

When 54MnCl2 was incubated with fresh bovine or caprine serum for 20 h and the serum subjected to electrophoresis at pH 9.5, the 54Mn bound to transferrin and alpha2-macroglobulin in proportions which varied with the temperature of incubation and the temperature of electrophoresis. Between 0 and 37 degrees C, the higher the temperature of incubation the larger the proportion bound to transferrin and the lower the proportion bound to alpha2-macroglobulin. The temperature at which electrophoresis was performed had little effect on the proportion of 54Mn bound to transferrin, but increasing temperature reduced the proportion of 54Mn bound to alpha2-macroglobulin. Mn2+ did not bind to purified transferrin in vitro in the absence of an oxidising agent. In the presence of permanganate, Mn3+ was formed and chelated by transferrin at physiological pH. In fresh serum this oxidation step may be performed by ceruloplasmin or molecular oxygen. Mn2+ was bound reversibly to alpha2-macroglobulin but this protein played no part in the oxidation of divalent manganese and had no effect on the protein binding of trivalent manganese. Manganese in the divalent state, either free as Mn2+ or bound to alpha2-macroglobulin, is removed from blood plasma very efficiently by the liver. However, the manganic-transferrin complex normally found in circulation is not rapidly removed from plasma. The liver can remove large amounts of excess manganous manganese which it presumably excretes; the small essential fraction of the manganese absorbed is oxidised to the trivalent state and bound to transferrin.
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PMID:Manganese metabolism in cows and goats. 6 Jan 37

A new case of analbuminemia is described for a six month old child of Algerian origin. The serum albumin concentration was 64 mg/l and its immunochemical action was identical to that of normal albumin. The system reacted by an increase of the synthesis of globulins. For the subject, the alpha1-antitrypsin, ceruloplasmin, haptoglobin, alpha2-macroglobulin, transferrin and immunoglobulins M contents were three times higher than the standard figures. However, it was possible to show that the presence of free bilirubin independent from proteins could be detected at a concentration of 17 mumol/l.
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PMID:[Biochemical modifications in a case of analbuminemia (author's transl)]. 6 Oct 76

All seven pure yolk sac tumors of gonadal and extragonadal origin tested showed a bright positive fluorescence for alpha-fetoprotein in the tumor tissue. A positive reaction was seen in both the tumor cells and the hyaline globules. In all cases, however, the positive fluorescence was distributed in some focal areas of the tumor tissue. Certain tumor cells showed a strong granular intracytoplasmic fluorescence, whereas others showed a weak or a negative fluorescence. The fluorescence-positive tumor cells were located mainly in the areas rich in fluorescence-positive hyaline globules. Besides alpha-fetoprotein, certain plasma proteins--albumin, alpha-1 antitrypsin, and transferrin--were also demonstrated in all five yolk sac tumors tested. The pattern of the distribution of positive fluorescence was basically similar to that of alpha-fetroprotein. Other plasma proteins--orosomucoid, haptoglobin, Gc-globulin, alpha-2 macroglobulin, hemopexin, and ceruloplasmin--were present in certain tumors, and were distributed mainly in a limited number of hyaline globules. Both IgG and IgA were present in two tumors of ovarian origin. The immunoglobulins were for the most part present in extracellular hyaline globules, suggesting that these are taken up from the circulation. Test for fibrinogen, beta-lipoprotein, IgM, IgE, beta-1C/beta-1A and beta-1E globulins were negative or questionable. In a hepatoblastoma, tests for alpha-fetoprotein were positive, but those for other plasma proteins were negative. Fine granular fluorescence was seen in each hepatocellular tumor cell. Mesenchymal elements were virtually unstained.
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PMID:Immunofluorescent demonstration of alpha- fetoprotein and other plasma proteins in yolk sac tumor. 6 8

The protein permeabilities of the blood-cerebrospinal-fluid barrier and the blood-urine barrier are compared. In both instances the permeation rates of proteins can be better correlated to hydrodynamic radii than to molecular weights. The decreasing clearance rates of ceruloplasmin, IgG, and IgA reflect the hydrodynamic heterogeneity of these proteins, which have similar weights. The IgM clearance rate appears too high, possibly owing to monomer IgM, other IgM fragments, selective transport, or active immunity, so its inclusion is not recommended in clearance studies.
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PMID:Hydrodynamic radii versus molecular weights in clearance studies of urine and cerebrospinal fluid. 6 19

Gene frequencies of the serum proteins third component of complement (C3) transferrin (Tf), haptoglobin (Hp), group specific component (Gc), serum cholinesterase (E1), alpha1-antitrypsin (Pi), beta2-glycoprotein I (Bg), and ceruloplasmin (Cp) in the Tajiks, Pushtoons, Hazaras, and Usbeks in Afghanistan were reported. Rare variants were observed in the C3, Tf, and Pi systems.
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PMID:Serum protein polymorphisms in four populations of Afghanistan. 6

The effect of a partially purified preparation of pig kidney alpha-L-fucosidase on some glycoproteins--human and rabbit gamma-globulin, glycoprotein from sheep submaxillary gland and ceruloplasmin--was studied. It was shown that the action of the enzyme of the glycoproteins was not accompanied by a release of fucose. A comparative study of the properties of free and concanavalin A-Sepharose 4B-bound alpha-L-fucosidase was done. The experimental data is indicative of difference in the pH-dependenced and thermostability of these two enzyme forms. It was found that bound alpha-L-fucosidase, similar to the free form, did not split off fucose from the native blood group substances. The data of isoelectric fucosing of alpha-L-fucosidase suggests the existence of enzyme polymorphism.
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PMID:[Substrate specificity and some properties of free and immobilized animal alpha-L-fucosidase]. 7 Feb 33


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