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Blood zinc

Rat (albino) 4 wk ad lib (W) Hemato 109 M (decreased ALAD activity and hemoglobin increased urinary excretion of ALA and increased blood zinc protoporphyrin) Flora etal. 1993 PbAc... [Pg.147]

Test results that show bioabsorption of toxicants (e.g., blood Pb levels) or reveal early medical effects of overexposure that do not constitute a disease entity (e.g., blood zinc protoporphyrin levels) can be given to the environmental engineer in personally identifiable form. Biological monitoring test results that identify a disease state (e.g., oligospermia) constitute confidential information about the health status of the individual which is not to be... [Pg.228]

Dilute plasma twenty-fold with 0.1 N HQ. For whole-blood zinc dilute one hundred-fold and for urine ten-fold with 0.1 N HQ. [Pg.337]

The normal zinc content of the body amounts to 20-30 mmol (1.3-2.0 g). The daily dietary requirement is 10-15 mg. In the blood, zinc is bound to tt2-macro-globulin, albumin or amino acids, and a small amount is also bound to transferrin. Zinc is crucial to a variety of enzyme reactions. This applies especially to the liver. More and more attention has therefore been paid to the role of zinc in liver disease in recent years. Six enzyme groups (hydrolases, isomerases, ligases, lyases, oxidore-ductases and transferases) with a total of 35 zinc metal-loenzymes are listed. (98) Almost 200 enzyme reactions in the body are zinc-dependent ... [Pg.50]

Zinc assumes a special role in the intrahepatic formation of retinol-binding protein, which is essential for the release of vitamin A into the blood. Zinc deficiency results in a decrease in RBR Furthermore, as a part of ADH, zinc is crucial for alcohol degradation in the hepatocytes and for enzyme activation in the detoxification of ammonia in the urea cycle, (s. fig. 3.12 )... [Pg.50]

Berfenstam, R., Studies on Blood Zinc, Acta Paediatr, Stockholm... [Pg.225]

Acrodermatitis Enteropathica. Acrodermatitis entero-pathica (AE) is characterized by periorificial and acral dermatitis, alopecia, and diarrhea. Patients with this disorder have abnormally low blood zinc levels (<30 Llg/dL) symptoms are reversed by oral zinc supplementation, with this being diagnostic.This formerly fatal condition is an autosomal recessive inborn error affecting zinc absorption from the intestinal mucosa, but the location of the gene defect has not yet been identified. [Pg.1140]

The objects of this study are the synthetic symmetrically substituted zinc(II)tetraphenylporphyrin (I) - ZnTPhP and the porphyrins of heme blood zinc(II) hematoporphyrin t.m.e.(II) - ZnHP, zinc(II)deuteroporphyrin IX d.m.e.(III) - ZnDP, zinc(II)protoporphyrin IX d.m.e. (IV) - ZnPP having different peripheral substitutes. [Pg.224]

Table 1 reports the zinc contents in blood of 730 roe deer harvested during the same hunting season in Siena County. The statistical parameters are shown for the entire sample as well as for subsamples based on the age and sex of the animals. On account of the limited home-range of this species, we could also relate the blood zinc values (as well as the Cu and Pb ones) of many animals to the lithology of the environment in whieh they lived. [Pg.492]

The effect of tin on heme biosynthesis appears to be dependent on the concentration of zinc (Chmielnicka et al. 1992). Oral administration of tin can affect the heme synthesis by inhibiting e-aminolevulinic acid dehydratase (ALAD) activity in blood. Zinc is required for ALAD activity and provides a protective role in heme synthesis by increasing the activity of ALAD. It is postulated that when the tin and zinc are coadministered, these metals are probably attaching to similar binding sites in the ALAD enzyme (Chmielnicka et al. 1992). [Pg.85]

Elucidation of some of the mechanisms of lead toxicity on the cellular and biochemical level has led to the development of several relatively sensitive biomarkers of lead exposure and toxicity, including measurements of the effects of lead on enzymes of the hematopoietic system. Lead-induced alterations in blood zinc protoporphyrin (ZPP) and erythrocyte 6-aminolevu-linic acid dehydratase (ALAD) activity have been established as relatively specific biomarkers of lead toxicity to the heme biosynthetic pathway (NRC 1993 USEPA 1986). Increases in blood ZPP occur as a result of inhibition of ferrochelatase (FC) by lead. Inhibition of ALAD by lead, which begins at a blood lead level of about 5 tg/dL (Chisolm et al. 1985 USEPA 1986), is considered to be one of the most sensitive biomarkers currently available. [Pg.30]

Atomic absorption using either flame or electrothermal atomization is widely used for the analysis of trace metals in a variety of sample matrices. Using the atomic absorption analysis for zinc as an example, procedures have been developed for its determination in samples as diverse as water and wastewater, air, blood, urine, muscle... [Pg.415]

Zinc. The 2—3 g of zinc in the human body are widely distributed in every tissue and tissue duid (90—92). About 90 wt % is in muscle and bone unusually high concentrations are in the choroid of the eye and in the prostate gland (93). Almost all of the zinc in the blood is associated with carbonic anhydrase in the erythrocytes (94). Zinc is concentrated in nucleic acids (90), and found in the nuclear, mitochondrial, and supernatant fractions of all cells. [Pg.384]

Copper-zinc-superoxide dismutase (from blood cell haemolysis) [9054-89-1J Mr 32,000... [Pg.523]

KELL blood group antigen is a plasma membrane protein isolated from red cells homologous to zinc-binding glycoproteins with neutral endopeptidase activity. [Pg.672]

The compounds of the t/block elements show a wide range of interesting properties. Some are vital to life. Iron is an essential component of mammalian blood. Compounds of cobalt, molybdenum, and zinc are found in vitamins and essential enzymes. Other compounds simply make life more interesting and colorful. The beautiful color of cobalt blue glass, the brilliant greens and blues of kiln-baked pottery, and many pigments used by artists make use of d-block compounds. [Pg.776]

Water soluble protein with a relative molecular mass of ca. 32600, which particularly contains copper and zinc bound like chelate (ca. 4 gram atoms) and has superoxide-dismutase-activity. It is isolated from bovine liver or from hemolyzed, plasma free erythrocytes obtained from bovine blood. Purification by manyfold fractionated precipitation and solvolyse methods and definitive separation of the residual foreign proteins by denaturizing heating of the orgotein concentrate in buffer solution to ca. 65-70 C and gel filtration and/or dialysis. [Pg.1493]

Zinc protoporphyrin in blood After 1 month exposure 2 50 pg/100 ml erythrocytes or lOOpg/IOOmI blood B... [Pg.98]

C04-0026. Cadmium ions are environmental pollutants found in mining waste, metal plating, water pipes, and industrial discharge. Cadmium ions replace zinc ions in biochemistry and cause kidney damage, high blood pressure, and brittle bones. Dissolved Cd " " impurities can be removed from a water sample... [Pg.235]

Carbonic anhydrase (CA) exists in three known soluble forms in humans. All three isozymes (CA I, CA II, and CA III) are monomeric, zinc metalloenzymes with a molecular weight of approximately 29,000. The enzymes catalyze the reaction for the reversible hydration of C02. The CA I deficiency is known to cause renal tubular acidosis and nerve deafness. Deficiency of CA II produces osteopetrosis, renal tubular acidosis, and cerebral calcification. More than 40 CA II-defi-cient patients with a wide variety of ethnic origins have been reported. Both syndromes are autosomal recessive disorders. Enzymatic confirmation can be made by quantitating the CA I and CA II levels in red blood cells. Normally, CA I and CAII each contribute about 50% of the total activity, and the CAI activity is completely abolished by the addition of sodium iodide in the assay system (S22). The cDNA and genomic DNA for human CA I and II have been isolated and sequenced (B34, M33, V9). Structural gene mutations, such as missense mutation, nonsense... [Pg.36]


See other pages where Blood zinc is mentioned: [Pg.225]    [Pg.228]    [Pg.65]    [Pg.70]    [Pg.95]    [Pg.493]    [Pg.88]    [Pg.225]    [Pg.228]    [Pg.65]    [Pg.70]    [Pg.95]    [Pg.493]    [Pg.88]    [Pg.292]    [Pg.400]    [Pg.665]    [Pg.340]    [Pg.373]    [Pg.385]    [Pg.55]    [Pg.113]    [Pg.324]    [Pg.882]    [Pg.79]    [Pg.85]    [Pg.67]    [Pg.104]    [Pg.149]    [Pg.154]    [Pg.390]    [Pg.97]    [Pg.9]    [Pg.54]    [Pg.156]    [Pg.47]   
See also in sourсe #XX -- [ Pg.1141 ]




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The determination of zinc in plasma, whole-blood and urine

Zinc in blood

Zinc in peripheral blood

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