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 optimum pH for ceruloplasmin as polyphenol oxidase (EC 1.10.3.2) activity was determined in human serum (pH 5.4) and the serum of conventional laboratory animals--the rat (pH 5.2), mouse (pH 5.2), hamster (pH 5.3), guinea pig (pH 5.4), multimammate mouse (pH 5.2) and rabbit (pH 5.4). Determined at the optimum pH in 0.1M acetate buffer polyphenol oxidase activity fell in the sequence: rat--man--rabbit--mouse--multimammate mouse--hamster--guinea pig. Ceruloplasmin polyphenol oxidase activity was inhibited by 0.1M phosphate buffer in the mouse, rat and multimammate mouse, but not in the other species. It was inhibited by 0.05M citrate and 0.1M phthalate buffer in all the species tested.
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PMID:Serum polyphenol oxidase activity (ceruloplasmin) in conventional laboratory animals and man. 2 13

The interaction of perphenazine and an ergoline derivative on estrogen-induced adenohypophyseal growth was studied in rats. Animals received perphenazine (Per; 2 mg) the ergoline derivative D-6-methyl-8-ergoline-(I)-yl acetic acid amide (200 mcg/rat/day), estradiol benzoate (EB; 1 mg) alone or in combination with 1 or more. Animals were killed after 3 weeks of treatment and adenohypophyses, thyroids, adrenals, testes, and seminal vesicles or ovaries and uteri were removed. Serum ceruloplasmin level and thyroxine binding to the adenohypophyseal proteins were determined. Estradiol induced marked growth of the adenohypophysis which was slightly potentiated by Per in males but significantly inhibited by the ergoline derivative in both sexes. When Per was given with the ergoline derivative the inhibitory effect was blocked. The ergoline derivative also inhibited the EB-induced increase in thyroxine-binding capacity of the adenohypophyseal proteins. However, in this instance, Per was ineffective in blocking this inhibition. Ceruloplasmin level which increased following EB administration was unaffected by administration of either Per or the ergoline derivative. In males, adrenal weight rose slightly after Per and markedly after EB. Testicular weight fell in all groups given EB and unaffected by the test drugs. Ovarian weight rose after administration of the ergoline derivative but the simultaneous administration of EB or Per prevented the increase.
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PMID:Interaction of perphenazine and an ergoline derivative on oestrogen-induced adenohypophyseal growth. 14 Mar 98

Starting from previous observations emphasizing an increased pseudocholinesterase (PCE) activity in obese and hyperlipemic subjects, the behaviour of this enzyme and of ceruloplasmin was studied in connection with changes of serum lipids and lipoproteins in various types of hyperlipoproteinemia. When compared to values detected in 67 middle-aged normal weight normolipemic subjects, PCE activity was found to be significantly greater (smaller than 0.001) in the 49 overweight subjects without obvious hyperlipemia but presenting a moderate increase of the prebeta electrophoretic fraction. PCE activity was much higher in lean or overweight subjects with endogenous hypertriglyceridemia (68 patients with type IV and 86 patients with mixed hyperlipemia). The slight increase of mean values of PCE activity in the 53 subjects with type II-a was due mainly to overweight subjects, while this enzyme's activity was not significantly changed in lean subjects with pure hypercholesterolemia. PCE activity was positively correlated with serum triglyceride (r equals 0.540; p smaller than 0.001) and the prebeta electrophoretic fraction (r equals 610; p smaller than 0.001). The correlation with beta-lipoproteins was not significant. Ceruloplasmin levels were not significantly changed. It is suggested that elevation of PCE activity could be connected to mechanisms leading to an increased secretion rate of lipoproteins.
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PMID:Serum pseudocholinesterase and ceruloplasmin in various types of hyperlipoproteinemia. 16 6

Three stages can be distinguished in the evolution of HA titer during Sendai virus multiplication in chorioallantoic membrane (CAM) fragments in relation to the age of CAM and conditions of inoculation and maintenance. Ceruloplasmin has an inhibitory effect on virus multiplication, more marked in the case of stationarily maintained CAM fragments and dependent on the relationship between the moment of ceruloplasmin addition and of virus inoculation. Maximum inhibition is achieved by inoculation of Sendai virus (1 Ha u) after 4 1/2-hour preincubation with ceruloplasmin (5 x 10(-7)M). The experimental data plead for the formation of a virus-ceruloplasmin complex able to inhibit both penetration and release of virus synthesized in the cell.
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PMID:Effect of ceruloplasmin on Sendai virus multiplication in chorioallantoic membrane fragments. 17 90

Ceruloplasmin (ferroxidase) the blue Cu-protein of vertebrate plasma, possesses significant oxidase activity towards Fe(II) and numerous aromatic amines and phenols. Its ferroxidase activity has led to the discovery that it is a molecular link between copper and iron metabolism. Ceruloplasmin mobilizes iron into the plasma from iron storage cells in the liver. An additional role of Cp may be as a contributor to the regulation of the balance of biogenic amines through its oxidase action on the epinephrine and the hydroxyindole series. Ceruloplasmin also serves as a major copper transport vehicle, comparable to transferrin for iron. Evidence is presented that the copper atoms of Cp are a prerequisite for copper utilization in the biosynthesis of cytochrome oxidase. The ability of Cp to release copper at specific cellular sites is believed to be related to its broad substrate spectrum of biological reducing agents. Thus Cp is a serum protein with several important functions, all of which are directly related to its oxidase activity.
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PMID:The biological role of ceruloplasmin and its oxidase activity. 18 81

Ceruloplasmin, the blue copper-protein of the blood plasma, is believed by some workers to be involved in the metabolic management of 5-hydroxytryptamine (serotonin) during pregnancy. 5-Hydroxytryptamine is abortifacient in experimental animals. By some authors, a role has been suggested for it in human abortion. The plasma concentrations of 5-hydroxytryptamine, copper and ceruloplasmin were measured in non-pregnant women, in normal early pregnancy and in cases of spontaneous abortion. Compared with normal early pregnancy, cases of inevitable abortion show lower values for both plasma copper and ceruloplasmin and higher values for plasma 5-hydroxytryptamine. The possible implications of these findings are discussed in view of the alterations in ceruloplasmin values in pregnancy and in the light of what is known of the pharmacology and metabolism of 5-hydroxytryptamine. It it believed that these alterations in plasma copper, ceruloplasmin and 5-hydroxytryptamine in cases of inevitable abortion are the effect, rather than the cause, of abortion.
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PMID:5-Hydroxytryptamine (serotonin), copper and ceruloplasmin plasma concentrations in spontaneous abortion. 26 87

Until now o-dianisidine was used as an indicator substance in a test system for the determination of diamine oxidase. More recently, however, this substance was also used to measure ceruloplasmin activity. A study of the test principles revealed that o-dianisidine was the one denominator for both enzymes. As it was found for diamine oxidase the indicator was oxidized via peroxidase mediated H2O2 cleavage. Ceruloplasmin, however, oxidized o-dianisidine directly with resulting free radical formation. An addition of histamine dihydrochloride or putrescine dihydrochloride to an incubation mixture, containing ceruloplasmin as enzyme and o-dianisidine or p-phenylene-diamine as substrates, produced an activation of the enzyme, being more than 10-fold in the presence of 1 X 10(-2) M putrescine at pH 7.0. It was assumed that an allosteric effect of the dihydrochloride component might be responsible for this activation. When the activity of purified diamine oxidase was determined by the o-dianisidine test and by the isotope assay, a very good correlation between both methods was found. But, in a mixture of diamine oxidase and ceruloplasmin, no differentiation between the two enzymic activities by the o-dianisidine test was possible. This observation demonstrated an interference of ceruloplasmin when the o-dianisidine method was used for the determination of diamine oxidase activity. To apply our findings also in vivo the amine oxidase activity increasing in guinea-pig plasma during inflammation, was determined by the o-dianisidine test and by specific methods for some amine oxidase. Despite an enhanced oxidation of the o-dianisidine observed, only an increase of ceruloplasmin activity was found. It was concluded that ceruloplasmin had no 'histaminase activity' as has been assumed by other authors using the o-dianisidine test.
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PMID:Determination of histaminase (diamine oxidase) activity by o-dianisidine test: interference of ceruloplasmin. 40 58

Radio gel and affin chromatography were used to study big gastrin interaction with blood proteins of man and animals. The experiments showed that big gastrin interacts with serum proteins in vitro. The gastrin-blood protein complex is labile and readily dissociates (T 1/2 = 8--14 min). A more stable complex is found in acidic medium. Ceruloplasmin is one of the blood serum proteins able to interact with big gastrin. The stability of hormone-protein complex, formed by gastrin and ceruloplasmin, is dependent upon hormone concentration. With the addition of C-terminal penta--and octapeptides to labelled hormone, binding increased. It is speculated that formation of labile gastrin-blood protein complexes is necessary for selective gastrin transport from hormone-producing cells to target cells.
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PMID:Interaction of synthetic human big gastrin with blood proteins of man and animals. 46 90

A detailed study was made of copper metabolism in rats during and after pregnancy and in the fetuses and pups up to the age of 6 wk. Maternal ceruloplasmin levels increase only briefly at the beginning of the third (and last) week of pregnancy. They then decrease to normal levels at term and decrease markedly in the early postpartum period. Bilary excretion of copper and 67Cu almost stops at term and remains decreased for 2 wk. In spite of this, there is no increase in hepatic copper levels. Except for a 1- to 2-day period shortly after delivery, maternal rats have a positive copper balance if lacteal elimination of copper is ignored. Levels of copper in milk drop at about the fourth day postpartum. Fetal hepatic copper levels are already above adult levels, but the concentration almost doubles during the first week after birth; it decreases to adult levels by 6 wk of age. Ceruloplasmin levels, which are found to be very low in the pups at birth, increase sharply in the first 24 h and quickly achieve adult levels. Large quantitative differences also occur between the pups and adults in concentrations of copper in the brain and kidney. Qualitative differences, measured with 67Cu, are most notable when the neonatal liver is compared with the adult liver.
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PMID:Copper metabolism in pregnant and pospartum rat and pups. 55 92

Ceruloplasmin, the blue copper-protein of vertebrate plasma, has been reviewed mainly from a functional point of view. However we have surveyed the chemistry and state copper in the molecule because of the implications of the recent data of Ryden (13,28). His observations suggest that unless special precautions are taken in the isolation of ceruloplasmin degradation, probably proteolytic, produces fragments of various sizes. When isolated, these fragments appear to be held together by noncovalent interactions. Comparison of their catalytic and spectral properties reveals no significant differences from a single homogeneous species of molecular weight of 134,000 isolated by Ryden's methods. On the other hand, the homogeneous molecule may differ in properties highly sensitive to conformation and three-dimensional parameters. Three types of copper atoms have been identified in ceruloplasmin, but their amino acid environment is still unknown. Ceruloplasmin possesses significant oxidase activity towards Fe(II) and numerous aromatic amines and phenols. Its ferroxidase activity has led to the discovery that it is a molecular link between copper and iron metabolism. Ceruloplasmin mobilizes iron into the plasma from iron storage cells in the liver. An equally important duty is that ceruloplasmin, after its rapid biosynthesis in the liver, serves as a major copper transport vehicle, comparable to transferrin. Evidence is accumulating that the copper atoms of ceruloplasmin are a prerequisite for copper utilization in the biosynthesis of cytochrome oxidase and other copper proteins. The ability of ceruloplasmin to release copper at specific cellular sites may be related to its broad substrate spectrum of biological reducing agents. A possible third role of ceruloplasmin is as a contributor to the regulation of the balance of biogenic amines through its oxidase action on the epinephrine and the hydroxyindole series. Thus ceruloplasmin is a copper-protein with several important functions, all of which are directly related to its oxidase activity.
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PMID:Ceruloplasmin: the copper transport protein with essential oxidase activity. 77 38


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