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Normal lactate

IV Mla Skin, subcutaneous tissue, or distant lymph nodes with normal lactate dehydrogenase Mlb Lung with normal lactate dehydrogenase Mlc To all other visceral sites (liver) or distant metastasis at any site with elevated serum LDH 7-19% 3-16%... [Pg.1433]

Without oxytocin-induced contraction, normal lactation cannot occur. At high concentrations, oxytocin has weak antidiuretic and pressor activity due to activation of vasopressin receptors. [Pg.844]

Data from a patient affected with a PDH defect are presented in Table 1.4.13. In general, hyperlactataemia (increasing with meals) associated with a normal lactate pyruvate ratio and normal ketonaemia is observed. The ketogenic diet is a rational treatment for PDH complex deficiency. [Pg.49]

Because of the short duration and severity of the metabolic acidosis, together with a near-normal lactate concentration, acid ingestion was the most likely cause for his acid-base disorder. This diagnosis was confirmed once the composition of the ingested fluid was known. [Pg.593]

Oxytocin alters transmembrane ionic currents in myometrial smooth muscle cells to produce sustained uterine contraction. The sensitivity of the uterus to oxytocin increases during pregnancy. Oxytocin-induced myometrial contractions can be inhibited by 13-adrenoceptor agonists, magnesium sulfate, or inhalation anesthetics. Oxytocin also causes contraction of myoepithelial cells surrounding mammary alveoli, which leads to milk ejection. Without oxytocin-induced contraction, normal lactation cannot occur. Oxytocin has weak antidiuretic and pressor activity. [Pg.875]

Prolactin is a polypeptide hormone (199 amino acids) whose major biological actions are related to normal lactation and reproduction. After hormone binding, signal transduction occurs via the cytokine receptor superfamily. It is well known... [Pg.445]

The normal lactate concentration in blood is between 1.2 and 2.7 mmol/1. For accurate lactate determination hemolysis of the sample is required to account for the (low) lactate content of erythrocytes. On the other hand, the glycolytic reactions in the sample have to be efficiently and rapidly inhibited in order to avoid lactate formation. Therefore the best-suited sample material is deproteinized blood however, the time period inevitably required for its preparation prevents rapid lactate assay. That is why the study of blood lactate sensors focuses not only on the sensor itself but also on the rapid pretreatment of blood samples. [Pg.304]

An equilibrium constant of 8.8 1.1 was obtained at 0.88-0.264 M H+. Oxy species of malic acid, ZrO(CH2CHOH(COO)2) and K2ZrO(CH2-CH0H(C00)2)2 406), and citric acid also are reported SOO). Polymeric lactate complexes have been reported by workers at Takeda Industries 551). Although a complete analysis was not given, the isolation of a polymer formulated as M4[Zr(O0HRCO2) ], where M is sodium or potassium and R is methyl or another alkyl, was reported. Blumenthal 63) has questioned whether the normal lactate will ever be formed. [Pg.45]

Accumulation of compounds related to the mitochondrial pathway can be detected in one or more body fluids of most patients [1, 2, 15]. Special attention has to be paid to the lactate concentration. Excess of lactate and alanine will be produced after reduction or transamination of accumulated pyruvate (see Fig. 27.1). If there is a severe block in the pyruvate oxidation pathway, and the produced lactate can not adequately be removed by peripheral tissues, it accumulates in blood, urine and/or cerebrospinal fluid, dependent upon the affected tissue(s). A decreased activity of the respiratory chain will shift the equilibrium of the lactate dehydrogenase reaction to conversion of pyruvate to lactate (see also Sect. 1). Thus, patients with a respiratory chain defect should demonstrate an increased lactate/pyruvate ratio in blood, whereas pyruvate dehydrogenase deficiency should result in a normal lactate/pyruvate ratio. However, this tool for differential diagnosis is not helpful in all cases. Furthermore, some patients do not accumulate lactate in blood or urine. [Pg.527]

Raised lactate and pyruvate — Normal lactate and pyruvate... [Pg.375]

Derivatives. The precise identification of a compound normally depends upon the preparation of a derivative and the determination of physical constants such as m.p. in the case of a solid. Many simple compounds can, however, be identified with a fair degree of certainty by intelligently-selected qualitative tests alone, e.g., formates, oxalates, succinates, lactates, tartrates, chloral hydrate. [Pg.402]

Thiamine requirements vary and, with a lack of significant storage capabiHty, a constant intake is needed or deficiency can occur relatively quickly. Human recommended daily allowances (RDAs) in the United States ate based on calorie intake at the level of 0.50 mg/4184 kj (1000 kcal) for healthy individuals (Table 2). As Httle as 0.15—0.20 mg/4184 kJ will prevent deficiency signs but 0.35—0.40 mg/4184 kJ are requited to maintain near normal urinary excretion levels and associated enzyme activities. Pregnant and lactating women requite higher levels of supplementation. Other countries have set different recommended levels (1,37,38). [Pg.88]

Lactate, a product of glucose catabolism in oxygen-starved muscles, can be converted into pyruvate by oxidation. What coenzyme do you think is needed Write the equation in the normal biochemical format using a curved arrow. [Pg.1173]

Analysis of ESRB 7 mice showed fewer and smaller litters than wild type mice as well as abnormal vascular function and hypertension. The reduction in fertility was attributed to reduced ovarian efficiency. Mutant females had normal breast development and lactated normally. Older mutant males displayed signs of prostate and bladder hyperplasia. s -2-deficient mice furthermore display diverse regulatory defects in the function of brain, lung, and white blood cells. The results indicated that ESRB is essential for normal ovulation efficiency but is not essential for lactation, female or male sexual differentiation, or fertility. [Pg.1130]

Plasma proteins are contraindicated in those with a history of allergic reactions to albumin, severe anemia, or cardiac failure in the presence of normal or increased intravascular volume and in patients on cardiopulmonary bypass. Plasma protein fractions are used cautiously in patients who are in shock or dehydrated and in those with congestive cardiac failure or hepatic or renal failure. These solutions are Pregnancy Category C drugp and are used cautiously during pregnancy and lactation. [Pg.635]

The dangers of shock are avoided or treated by intravenous infusion of large volumes of a salt-containing solution that is isotonic with blood (has the same osmotic pressure as blood), usually one known as lactated Ringer s solution. The added liquid increases blood volume and blood flow, thereby improving oxygen delivery. The HCO / H2C03 ratio then increases toward normal and allows the severely injured person to survive. [Pg.573]

Glycogenosis type VIII (phosphorylase b kinase deficiency) gives rise to myopathy and liver disease, either singly or in combination. Phosphorylase b kinase (PBK) converts the inactive b form of both muscle and liver phosphorylases to the active a forms of the enzymes. The ischemic lactate test sometimes shows a flat result as in McArdle s disease, but is more likely to be normal. Histochemical demonstration of myophosphorylase activity in tissue sections shows a near-normal reaction due to the presence of phosphorylase a. Accumulation of glycogen is modest and found mainly in type 2 (fast-twitch glycolytic) muscle fibers. [Pg.302]

Figure 7-11. Normal and pathologic patterns of lactate dehydrogenase (LDH) isozymes in human serum. LDH isozymes of serum were separated by electrophoresis and visualized using the coupled reaction scheme shown on the left. (NBT, nitroblue tetrazolium PMS, phenazine methylsulfate). At right is shown the stained electropherogram. Pattern A is serum from a patient with a myocardial infarct B is normal serum and C is serum from a patient with liver disease. Arabic numerals denote specific LDH isozymes. Figure 7-11. Normal and pathologic patterns of lactate dehydrogenase (LDH) isozymes in human serum. LDH isozymes of serum were separated by electrophoresis and visualized using the coupled reaction scheme shown on the left. (NBT, nitroblue tetrazolium PMS, phenazine methylsulfate). At right is shown the stained electropherogram. Pattern A is serum from a patient with a myocardial infarct B is normal serum and C is serum from a patient with liver disease. Arabic numerals denote specific LDH isozymes.

See other pages where Normal lactate is mentioned: [Pg.302]    [Pg.132]    [Pg.240]    [Pg.3957]    [Pg.219]    [Pg.155]    [Pg.468]    [Pg.328]    [Pg.637]    [Pg.305]    [Pg.102]    [Pg.187]    [Pg.1776]    [Pg.302]    [Pg.132]    [Pg.240]    [Pg.3957]    [Pg.219]    [Pg.155]    [Pg.468]    [Pg.328]    [Pg.637]    [Pg.305]    [Pg.102]    [Pg.187]    [Pg.1776]    [Pg.149]    [Pg.174]    [Pg.180]    [Pg.384]    [Pg.64]    [Pg.95]    [Pg.632]    [Pg.121]    [Pg.117]    [Pg.521]    [Pg.548]    [Pg.636]    [Pg.251]    [Pg.300]    [Pg.302]    [Pg.118]    [Pg.126]    [Pg.126]    [Pg.57]   
See also in sourсe #XX -- [ Pg.47 ]




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