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 reaction of serum samples with bromcresol green proceeds in two steps. Albumin is responsible for the faster (less than 1 min) reaction; the slower (30-min) reaction is a measure of "acute phase reactant(s)" in serum. Serum is simply mixed with bromcresol green reagent and the absorbance is measured twice, immediately and at 60 min. Albumin concentrations, determined from the absorbance at 0 min, correlate well with those determined by Laurell "rocket" immunoelectrophoresis; r = 0.95 with no certain deviation from unity for the slope and with a negligible difference at zero concentration. The slow reaction was expressed as deltaA% = 100 (deltaAs/deltaAv) where deltaAs and delta Av are the changes in absorbance between 60 and 0 min for the sample and a commercial control serum, respectively. The value for deltaA% correlates well with the percentage of alpha2-fraction as determined by electrophoresis on cellulose acetate, as well as with orosomucoid and ceruloplasmin, all of which are acute phase reactant(s). Whether these proteins or other acute phase reactant(s) actually cause the slow reaction has not yet been established.
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PMID:Improved specificity of serum albumin determination and estimation of "acute phase reactants" by use of the bromcresol green reaction. 0 38

The effect of anion binding to ceruloplasmin has been studied using absorption and cirbular dichroism spectral data. At anion to ceruloplasmin molar ratios approaching infinite, OCN-, N3- and SCN- bind to ceruloplasmin giving rise to similar alterations in circular dichroism and absorption spectra. The positive bands at 610 and 520 nm in circular dichroism spectra disappear, a negative one apperars at 600 nm and the peak at 450 nm is only slightly modified. There is a new negative band at 410 nm well-defined in OCN- ceruloplasmin spectra. The decrease in absorption at 610 nm is ascribed to the disruption of one type I Cu-S(cysteine) bond owing presumably to the changes induced by anions in the protein secondary structure. The new band at 410 nm is assigned to a charge transfer transition from the ligand replacing cysteine at its binding site. Both absorption and circular dichroism spectra show isobestic points indicating that anion binding to the enzyme, disruption of one of the two type I Cu-S bonds and coordination of this Cu to another protein residue take place simultaneously.
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PMID:Ceruloplasmin-anion interaction. A circular dichroism spectroscopic study. 0 18

The relationship between differences in the clinical polymorphism of hepatolenticular degeneration (Wilson's disease) and characteristics of CP (ceruloplasmin) structural changes were investigated. The comparative study of Wilson's disease patients revealed two forms of clinical development of this disease which differ from each other by the expression of the visceral symptoms preceding the establishment of the typical neurological picture. The peptide map analysis of tryptic hydrolysates of the CP from individual patients has demonstrated the altered peptide patterns in five cases. Clinical and genetic heterogeneity of Wilson's disease is discussed.
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PMID:[Clinical polymorphism and ceruloplasmin variants in hepatolenticular degeneration]. 2 Nov 23

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

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

Preincubation of Sendai virus with ceruloplasmin induced in chorioallantoic membrane (CAM) fragments the synthesis of a population with decreased infectivity and high haemagglutinating (HA) and neuraminidase (NA) activities, whereas preincubation with solubilized virus envelopes led to the production of a viral population with the same infectivity as the control, but with lower HA and NA activities. Preincubation of the virus with a mixture of ceruloplasmin and solubilized envelopes depressed the overall virus synthesis; the resulting population had a low infectivity and high HA and NA activities. The variation in the HA/NA ratio indicates a modification in the envelope structure.
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PMID:Sendai virus multiplication in the presence of ceruloplasmin and homologous virus envelopes. 4 34

Genetic studies in the Markham Valley, northeastern Papua New Guinea; Gamma globulin (Gm and Inv), group specific component (Gc) and ceruloplasmin (Cp) typing. M. S. Schanfield, Eugene Giles and H. Gershowitz, Department of Human Genetics, University of Michigan, Ann Arbor, Michigan 48104. Immunoglobulin allotyping was carried out on 680 serum samples from inhabitants of the Markham Valley, Papua New Guinea (seven villages speaking the same Melanesian [PAP] speaking village). Family and population data verified the presence of Gm-ag, G-ab and Gm-afb among the MN speakers and Gm-ag, Gm-axg, Gm-ab and Gm-afb among the PAP speakers. The frequency of Gm-ag was between 0.048 and 0.235, while the frequency of Gm-ab was between 0.427 and 0.627 and the frequency of Gm-afb ranged between 0.261 and 0.424 among the seven MN villages; the single PAP village had frequencies of 0.568, 0.160, 0.213 and 0.059 for Gm-ag, Gm-axg, Gm-ab and Gm-afb respectively. The frequency of Inv1 ranged between 0.034 and 0.095 in the MN villages and 0.014 in the PAP village. The rare occurrence of Gm(x) without Gm(g) was explained by the presence of a Gm-axfb haplotype, while in two PAP families the presence of Gm(x) without Gm(g) was explained by the abnormally weak expression of Gm(g) in a Gm-axg haplotype. A total of 654 sera were typed for Gc, with the seven MN villages ranging between 0.350 and 0.650 for Gc-1, 0.312 and 0.575 for Gc-2 and between 0.017 and 0.112 for Gc-Ab; the single PAP village had a value of 0.627 for Gc-1, 0.165 for Gc-2 and 0.208 for Gc-Ab. A total of 693 sera were tested for ceruloplasmin type. All showed the common Cp(b) phenotype.
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PMID:Genetic studies in the Markham Valley, northeastern Papua New Guinea: gamma globulin (Gm and Inv), group specific component (Gc) and ceruloplasmin (Cp) typing. 4 22

In our hands the dianisidine technique for the staining of ceruloplasmin in polyacrylamide gels following disc electrophoresis has proven unsatisfactory for three reasons. First, staining of ceruloplasmin could not be achieved with physiological amounts of the glycoglobulin present in serum. Second, even when relatively massive quantities of pure ceruloplasmin permitted effective staining there was loss of stain intensity with increasing electrophoresis time. Third, the necessity of utilizing dianisidine in alcoholic solution produces undesirable shrinkage and distortion of the gels. However, a modification of the p-phenylenediamine technique for the staining of ceruloplasmin in agar gels has been found to stain ceruloplasmin very effectively in polyacrylamide gels following disc electrophoresis.
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PMID:Observations on the staining of ceruloplasmin following disc-electrophoresis utilizing polyacrylamide gels. 4 75

Human ceruloplasmin from fresh serum has been purified by chromatography on hydroxyapatite and Con A-Sepharose. Quantitative immunoelectrophoretic analysis of fresh serum, stored serum and fractions from the different purification steps for human ceruloplasmin has been carried out. A combination of the latter, advanced technique with amino acid analysis, molecular weight determination by size chromatography, urea treatment, staining for oxidase activity and enzymatic proteolysis, has revealed that: 1) human cerulplasmin is a heterogeneous mixture of two glycoproteins (x) differing only in their carbohydrate content and 2) the protein part contains at least one very labile peptide bond which upon enzymatic hydrolysis gives rise to peptides with molecular weights of 93,000 (y) and 24,000 (z) dalton, respectively. The two glycoproteins are immunochemically identical. The y peptide is immunochemically partially identical, and the z peptide immunochemically non-identical, with the parent molecule. The y and z peptides are non-identical. On the basis of these observations a simplified two-dimensional model of human ceruloplasmin is proposed.
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PMID:Immunochemical investigation on human ceruloplasmin. Partial explanation of the "heterogeneity". 4 18

Various CSF proteins were studied in 255 definite multiple sclerosis patients at various disease stages and compared with corresponding values obtained from 174 controls. The CSF changes in acute multiple sclerosis patients included a significant increase of total proteins and of gamma globulin, IgG, IgA, IgM, alpha-2 ceruloplasmin, 7S-gamma-1, and cytotoxic index for nerve cells in tissue culture, and significant decreases of pre-albumin, alpha-1, and alpha-2 and of the beta/gamma globulin ratio. The CSF levels of IgG, IgA, and IgM remained significantly higher in steroid-treated multiple sclerosis patients than in controls, but the levels often were significantly reduced while patients were on treatment or in remission. During remission or treatment with ACTH and/or steroids, the alpha-2 ceruloplasmin, 7S-gamma-1, and cytotoxic index were significantly reduced and the pre-albumin, alpha-1, and alpha-2 globulin classes and the beta/gamma ratio showed a tendency to return to normal.
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PMID:Cerebrospinal fluid proteins in multiple sclerosis. 4 11


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