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Serum components transferrin

Whilst growth factors in the serum provide specific proliferative stimuli, studies with cultured cells have indicated other important components for cell proliferation [18]. For example, insulin is required to facilitate glucose and amino-acid uptake, and transferrin, which binds iron, makes it available to the cell. Serum is also believed to supply trace elements such as selenium, copper and zinc as well as fatty acids important for cell growth. Some serum components such as ascorbate, a-tocopherol, caeruloplasmin and albumin may serve important antioxidant functions [19]. [Pg.157]

Breuer W, Ermers MJJ, Pootrakul P, Abramov A, Hershko C, Cabantchik ZI. Desferrioxamine-chelatable iron, a component of serum non-transferrin-bound iron, used for assessing chelation therapy Blood 2001 97 792-8. [Pg.1202]

F9 embryonal carcinoma cells have a simple set of growth supplements which are required for growth in serum-free medium insulin, transferrin, and fibronectin (Rizzino and Sato, 1978). Fibronectin is a component of the extracellular matrix and facilitates the attachment of the cells to the culture dish. In addition, high density lipoprotein (HDL) has been observed to promote the growth of F9 cells serum-free. [Pg.473]

Cell Culture-Derived Media-Derived Protein Impurities. Immunoassays can detect low impurity levels (<1 ppm).4 The ELISA is probably one of the most sensitive analytical methods. If bovine serum is used as a media component, then testing should include ELISAs for bovine serum albumin (BSA), bovine transferrin, bovine fetuin, and bovine IgG. Often hormones and growth factors, such as insulin or insulinlike growth factor, are used as media components. ELISAs should be used to detect and quantitate these residuals in the various production steps as well as in the final product. There are commercially available antibodies to most commonly used media components. If proprietary media components are used, then the same investment in time and effort is required for the production of specific antibodies, as described above for host cell impurities. [Pg.291]

Determination of acute-phase proteins (CRP, orosomucoid, haptoglobin, transferrin, prealbumin), immunoglobulins (IgA, IgG, IgM), compressive markers (albumin, fibrinogen), markers of tissue destruction (Apo A-I, A-II, Apo B), components of complement (C3, C4), proteinase inhibitors (antithrombin HI, a -antitrypsin). The measurement was performed simultaneously in CSF and in serum (plasma) by a laser nephelometric method. The functional state of the blood-CSF barrier was evaluated numerically with the help of the quotient Q = Albcsp/s and also by the intrathecal synthesis of immunoglobulins according to Reiber s formula and for each class—IgG, IgM, IgA. [Pg.38]

Efficacy is appreciated clinically and has two distinct components. Initially there is reversal in the impaired effort tolerance that parallels regeneration of the haemoglobin levels. This is followed by a longer period when cognitive function gradually improves after stores are reconstituted. Oral iron typically needs to be given between 3 and 6 months and certainly until both percentage saturation of transferrin and serum, or preferably red cell, ferritin are normal. It is furthermore prudent that treated indi-... [Pg.731]

Mechanism of Action An enzymatic mineral that is an essential component in the formation of Hgb, myoglobin, and enzymes. Promotes effective erythropoiesis and transport and utilization of oxygen (Oj). Therapeutic Effect Prevents iron deficiency. Pharmacokinetics Absorbed in the duodenum and upper jejunum. Ten percent absorbed in patients with normal iron stores increased to 20%-30%in those with inadequate iron stores. Primarily bound to serum transferrin. Excreted in urine, sweat, and sloughing of intestinal mucosa. Half-life 6 hr. [Pg.495]

The relationship of lactotransferrin to serum transferrins is more obscure. Derechin and Johnson (33) found that bovine lactotransferrin had two distinct immunologic components, one of which reacted similarly to blood serum transferrin and one which did not react with blood serum transferrin. Komatsu et al. (83) found immunologic cross reactivity between human serum transferrin and human lactotransferrin, but the cross reactivity was not strong. [Pg.195]

Variations in the transferrins within a species have been studied in detail for the chicken. Lush (89), reported two components of ovotransferrin when chicken egg white was subjected to starch gel electrophoresis. This observation has been confirmed by Williams (136), Ogden et al. (101) and Feeney et al. (38). Odgen et al. (101) reported that the chicken egg whites varied genetically. The B type consisted of two components as observed by Lush and other investigators. The A type had two components, the slower of which was coincident with the faster component of type B. The AB type also existed and showed three bands electrophoreti-cally. These authors also reported corresponding variations in the serum transferrins of this particular strain of chickens. [Pg.197]

The tandem crossed method (Kroll, J., Scand. J. Clin. Lab. Invest., 22, 79, 1979) is another way to identity a specific component in a mixture. Figure 28-11, p. 344, shows the spotting template and the results. "It is essentially the same as crossed immuno-electrophoresis except that two samples are applied in the first dimension gel, the sample wells having a centre to centre distance of 10 mm." Again using transferrin as the example, "Human serum, 2 pL, is applied in the rear sample well and 4 pL of the pool containing the pure human transferrin is applied in the other well in the... [Pg.343]

The growth of the embryo proper clearly depends on the extraembryonic membrane, but a well-developed membrane did not in itself lead to high levels of embryo growth. Indeed, this disparity between embryo and extraembryonic membrane growth was noted with serum, conalbumin, and the yolk livetin and transferrin fractions. A protein such as ovalbumin or lipovitellin appears to be a necessary component in order to achieve favorable embryo growth. The inability to replace ovalbumin with bovine serum albumin suggests that this requirement has some... [Pg.316]


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See also in sourсe #XX -- [ Pg.34 , Pg.168 , Pg.193 ]




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