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)

The catalytic activity of phosvitin in Fe(II) oxidation and the addition of iron to transferrin were studied under various conditions. It was concluded that the Fe(II) oxidized by phosvitin would bind to apotransferrin, although an appreciable fraction of Fe(III) remained bound to phosvitin. Fe(III) also migrated from phosvitin to apotransferrin. This reaction was first-order with respect to Fe(III)-phosvitin concentration with a half-time (t1/2) of 10 min, and a first-order rate constant, k=0.069min-1, in 700 muM-phosphate buffer, pH 7.2, at 30 degrees C. The catalysis of the oxidation of Fe(III) by phosvitin was proportional to O2 concentration, and is quite different from the relative O2 independence of Fe(II) oxidation as catalysed by ferroxidase. A scheme for the mobilization and transfer of iron in the chicken, including the role of ferroxidase, phosyitin and transferrin, is presented.
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PMID:Iron oxidation and transferrin formation by phosvitin. 0 72

Many specific plasma proteins show dose-related changes when oral estrogens are administered. Large increases in concentration are seen in many important binding proteins, such as the sex hormone-binding globulin, transcortin, the retinol-binding protein, ceruloplasmin, and transferrin. A smaller group of plasma proteins are reduced in amount. These changes are related to altered rates of hepatic synthesis and secretion. As the overall effect of estrogen is one of increased protein synthesis, there is a reduction in the amount of plasma-free amino acids and in the pattern of distribution. Oral contraceptive (OC) users frequently show significant alterations in biochemical tests of vitamin status, at least some of which are related to alterations in plasma proteins. Other biochemical changes associated with OC use include a fasting hyperlipidemia, due mainly to increases in triglycerides, although there is often also a small increase in cholesterol. These changes are due primarily to increases in several lipoprotein fractions and are related mainly to the estrogen component. A deterioration in glucose tolerance occurs in many OC users and is probably induced by both estrogens and progestogens. There is evidence that certain clinical side effects of OCs, such as depression, are associated with specific biochemical changes.
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PMID:Biochemical basis for the selection of oral contraceptives. 3 19

The serum concentrations of the acute phase proteins, C-reactive protein, caeruloplasmin and haptoglobin were significantly higher in children with protein-calorie malnutrition than in age-matched controls, while the concentrations of alpha1 antitrypsin, alpha2 macroglobulin, transferrin and complement component C3 were significantly lower. During rehabilitation and treatment with antibiotics, C-reactive protein disappeared from the serum in most of the patients whilst the levels of caeruloplasmin and haptoglobin returned to normal values. On the other hand the serum concentration of alpha1 antitrypsin, alpha2 macroglobulin, transferrin and C3 showed significant increases. It is suggested that C-reactive protein and haptoglobin may provide useful indices of the presence or absence of infection in children with malnutrition.
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PMID:Acute phase proteins in children with protein-calorie malnutrition. 5 43

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

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

Serum protein components were evaluated by the specific radial immunodiffusion technique in a number of protein energy malnourished infants and young children, as well as in a group of parallel controls. Results show a drop in both serum prealbumin and albumin in concordance with the severity of the condition in both KWO and marasmus. Serum level of varies as 1-acidic glycoprotein was elevated, being more marked in KWO than in marasmus. Serum oc1-antitrypsin, haemopexin, ceruloplasmin and transferrin were all reduced but to a varying extent in both KWO and marasmus. The levels of serum IgA and IgM were above normal in all disease entities except for a slight decrease of IgA in 2nd grade marasmus. On the other hand, serum IgG was reduced in the majority of cases. The ratio of serum cerutoplasmin to transferrin in KWO was found to be of diagnostic value in different grades of the disease.
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PMID:Quantitative immunodiffusion assay of serum protein patterns in protein calorie malnutrition (PCM). 7 40

In the serum of 27 patients with malignant lymphogranulomatosis the authors determined the serum level of glycoproteid-carbohydrate components (hexose, hexosamine, sialin acid, and seromucoid) and the concentration of 11 different glycoproteids. In the early stage of the disease the immunoglobulin level is moderately increased in the serum, whereas a diminution can be observed in stage IV. The concentrations of ceruloplasmin, alpha-2-macroglobulin and orosomucoid were already increased significantly in stage III. The increase did not continue in stage IV. In the final stage of the disease the concentrations of alpha-1-antitrypsin and haemopexin turned out to be increased considerably. A significant decrease in the transferrin level could be registered in stage III with this diminution also continuing in the further course. Changes of beta-C-globulin and haptoglobin concentrations could not be evaluated statistically. The content of carbohydrate components in the glycoproteids will already increase in the early stage of the disease with this increase continuing in the further course. Among histological types there was a more significant increase of immunoglobulins in those forms rich of lymphocytes.
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PMID:[Immunoglobulins and glycoproteins in lymphogranulomatosis]. 8 Mar 59

In thirty children hospitalized with acute benign, short-duration gastroenterocolitis, no obligate pathogens were isolated from stools. Five bleedings were established from each patient in order to obtain the protein profiles of albumin, orosomucoid, haptoglobin, alpha2-macroglobulin, ceruloplasmin, transferrin, C3-component, C-reactive protein, immunglobulins IgG, IgA, IgM and IgD. The proteins were quantitated by the single radial immunodiffusion method. The initial drop in some of the proteins followed may be related to general protein loss, negative nitrogen balance or hemodilution. The absence of a significant increase in all the investigated immunoglobulin classes contrasted with remarkable increase in haptoglobin and orosomucoid, both reaching normal levels in late convalescence. C-reactive protein could be demonstrated in half of the children showing early normalization with disappearance of clinical symptoms. In contrast to ceruloplasmin and C3- component, alpha2-macroglobulin was not involved in the acute phase protein reaction.
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PMID:Twelve serum protein profiles in children with acute nonbacterial gastroenterocolitis. 8 77


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