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Affecting Blood

The ability of L-tryptophan to bind to plasma proteins of the blood and circulate as free and bound tryptophan is a unique feature for an amino acid. This binding is affected by and competes with other compounds that bind plasma proteins, such as nonesterified fatty acids (NEFA) and certain drugs. This relationship in blood affects its transport from the blood to the brain because only the free tryptophan is transplanted through the blood-brain barrier. Free tryptophan s concentration in blood in relation to other amino acids, particularly branched-chain amino acids (BCAA), affects its transport to the brain. [Pg.252]

Through this sequence of relationships the concentration of CO2 in the blood affects the blood pH. [Pg.257]

The concentration of nutrients or metabolites in the blood affects the rate at which they are used and stored in different tissues ... [Pg.478]

HUMAN HEALTH RISKS EPA RfD 0.0002 mg/kg/d EPA cancer risk level 8E-7 mg/m EPA Group B2 probable human carcinogen Acute Risks eye and skin irritation possible nervous system disturbances drowsiness incoordination hallucinations confusion peripheral neuropathy Chronic Risks carcinogen nerve damage damage to cardiovascular system reddish rash adverse blood affects. [Pg.9]

ACUTE HEALTH RISKS irritation of eyes, nose and throat may eause effects on the blood affects central nervous system eye lacrimation cough pulmonary changes headache dizziness drowsiness confusion weakness abdominal pain nausea vomiting unconscious-... [Pg.724]

Absorption route Can enter the body by inhalation or ingestion. Evaporation negligible at 20°C, but harmful atmospheric concentrations can build up rapidly if heated or in the form of airborne particles. Immediate effects Irritates the eyes, skin and respiratory tract. Effects of prolonged/repeated exposure Can affect the blood. Affects the blood vessels. In serious cases risk of death. ... [Pg.810]

In what way is the available calcium level in the blood affected by phosphate levels ... [Pg.38]

Interferons (lENs) (52,53), a family of species-specific vertebrate proteins, confer nonspecific resistance to a broad range of viral infections, affect cell proliferation, and modulate immune responses. AH three principal interferons, a-interferon (lEN-a) produced by blood leucocytes, P-interferon (lEN-P) by fibroblasts, and y-interferon (lEN-y) by lymphocytes, also have antiviral activity. The abiUty of interferons to inhibit growth of transplantable and carcinogen-induced tumor led to research showing the direct antiproliferative and indirect immune-mediated antitumor activities (see Chemotherapeutics, anticancer). IENs have been found to be efficacious in certain malignancies and viral infections, eg, hairy cell leukemia (85% response) and basal cell carcinoma (86% response). However, the interferons do have adverse side effects (54). [Pg.40]

Exposure to excessive amounts of lead over a long period of time (chronic exposure) increases the risk of developing certain diseases. The parts of the body which may be affected include the blood, nervous system, digestive system, reproductive system, and kidneys. These effects include anemia, muscular weakness, kidney damage, and reproductive effects, such as reduced fertiHty in both men and women, and damage to the fetus of exposed pregnant women. [Pg.52]

Alkyl mercury compounds in the blood stream are found mainly in the blood cehs, and only to a smah extent in the plasma. This is probably the result of the greater stabhity of the alkyl mercuric compounds, as well as their pecuflar solubiUty characteristics. Alkyl mercury compounds affect the central nervous system and accumulate in the brain (17,18). Elimination of alkyl mercury compounds from the body is somewhat slower than that of inorganic mercury compounds and the aryl and alkoxy mercurials. Methylmercury is eliminated from humans at a rate indicating a half-life of 50—60 d (19) inorganic mercurials leave the body according to a half-life pattern of 30—60 d (20). Elimination rates are dependent not only on the nature of the compound but also on the dosage, method of intake, and the rate of intake (21,22). [Pg.116]

The development of easy-to-use assays for determining theophylline blood levels afforded a handle on maintenance of effective but nontoxic levels. The relatively good availabihty of such assays in the United States probably contributed to the historical preference for theophylline treatment by U.S. physicians. Careful titration of the dose must be done on a patient-by-patient basis because individual rates of metaboHsm vary widely. Most ( 85%) of an oral dose of theophylline is metabolized by Hver microsomal enzymes. As a result many dmgs, eg, cimetidine [51481-61-9], anticonvulsants, or conditions, eg, fever, cigarette smoking, Hver disease, which affect Hver function alter theophylline blood levels. [Pg.440]

The notion that complex carbohydrates eHcit a gradual, steady secretion of insulin while sugars cause a sudden release of this hormone accompanied by a rapid drop in blood glucose has fostered the behef that hypoglycemia is affected by sucrose ingestion. However, research does not support this conclusion (63). [Pg.6]

The symptoms of vitamin E deficiency in animals are numerous and vary from species to species (13). Although the deficiency of the vitamin can affect different tissue types such as reproductive, gastrointestinal, vascular, neural, hepatic, and optic in a variety of species such as pigs, rats, mice, dogs, cats, chickens, turkeys, monkeys, and sheep, it is generally found that necrotizing myopathy is relatively common to most species. In humans, vitamin E deficiency can result from poor fat absorption in adults and children. Infants, especially those with low birth weights, typically have a vitamin E deficiency which can easily be corrected by supplements. This deficiency can lead to symptoms such as hemolytic anemia, reduction in red blood cell lifetimes, retinopathy, and neuromuscular disorders. [Pg.147]


See other pages where Affecting Blood is mentioned: [Pg.3]    [Pg.463]    [Pg.1351]    [Pg.553]    [Pg.553]    [Pg.454]    [Pg.582]    [Pg.19]    [Pg.39]    [Pg.521]    [Pg.3]    [Pg.463]    [Pg.1351]    [Pg.553]    [Pg.553]    [Pg.454]    [Pg.582]    [Pg.19]    [Pg.39]    [Pg.521]    [Pg.206]    [Pg.1150]    [Pg.294]    [Pg.442]    [Pg.234]    [Pg.520]    [Pg.154]    [Pg.172]    [Pg.200]    [Pg.52]    [Pg.93]    [Pg.298]    [Pg.188]    [Pg.85]    [Pg.227]    [Pg.95]    [Pg.407]    [Pg.430]    [Pg.470]    [Pg.474]    [Pg.496]    [Pg.292]    [Pg.317]    [Pg.46]    [Pg.228]    [Pg.215]    [Pg.217]   
See also in sourсe #XX -- [ Pg.30 ]




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Drugs used to affect blood coagulation

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