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Glycoproteins serum, human

Takahasfai N, Takahashi Y, Putnam FW. Periodidty of leucine and tandem repetition of a 24-amino add segment in the primary structure of leucine-ridi a2-glycoprotein of human serum. Proc Natl Acad Sd U S A 1985 82 1906-10. [Pg.155]

E Brunner and W. E. Muller, Prazosin binding to human aj-add glycoprotein (orosmucoid), human serum albumin, and human serum. Further characterisation of the single drug binding site of orosmucoid, /. Pkarm. Pharmacd.. 37 305 (1985). [Pg.357]

Williams, I.P., Rich, B. and Richardson, P.S. (1983). Action of serum on the output of secretory glycoproteins from human bronchi in vitro. Thorax 38, 682-685. [Pg.167]

The transferrins are all glycoproteins, and human serum transferrin contains about 6 percent carbohydrate. These carbohydrate groups are linked to the protein, and apparently strongly affect the recognition and conformation of the native protein. [Pg.18]

J. Hermansson et al.. Chiral HPLC separations of vinca alkaloid analogues on al-acid glycoprotein and human serum albumin columns, J. Chromato., 609(1992)163. [Pg.469]

CHIRAL-AGP CHIRAL-CBH CHIRAL-HAS a 1-acid glycoprotein cellobiohydrolase human serum albumin Used in wide pH range CHROMTECH... [Pg.49]

Although few studies have been carried out for Cd speciation in biological fluids (e.g., human serum, human milk, cow milk, and formula milk), in cow and formula milk Cd seems to be bound to caseins while in human serum Cd appears to be complexed by ceruloplasmin, a well-known glycoprotein for metal storage. [Pg.328]

The occurrence and composition of the glycoproteins in human blood serum have been reviewed by Winzler (5). Evidence for the existence of at least four such materials has been obtained by Schmid 79). One of these is present in serum to the extent of 0.5 % and is the principal glycoprotein of the ai-globulin fraction. [Pg.725]

Proteins. A chiral stationary phase with immobilized a -acid glycoprotein on silica beads was introduced by Hermansson in 1983 [18, 19]. Several other proteins such as chicken egg albumin (ovalbumin), human serum albumin, and cellohy-drolase were also used later for the preparation of commercial CSPs. Their selectivity is believed to occur as a result of excess of dispersive forces acting on the more retained enantiomer [17]. These separation media often exhibit only modest loading capacity. [Pg.58]

The resolution of these columns for protein mixtures, however, was comparably poor. The peak capacity for human serum albumin was near 3 during 20 min gradient elution. Improvement has been reached by covalent binding of PEI (M = 400-600) onto a 330 A silica of 5 pm particle size [38], The peak capacities of ovalbumin and 2a -arid glycoprotein were 30-40 (tgradienl = 20 min). Enhanced peak capacity and resolution probably were due to the more diffuse structure of PEI coupled to silane moieties than that of strictly adsorbed on silica and cross-linked (see Sect, 2.2). Other applications of covalently adsorbed PEI are discussed in Sect. 4.1. [Pg.147]

There is a wide variety of commercially available chiral stationary phases and mobile phase additives.32 34 Preparative scale separations have been performed on the gram scale.32 Many stationary phases are based on chiral polymers such as cellulose or methacrylate, proteins such as human serum albumin or acid glycoprotein, Pirkle-type phases (often based on amino acids), or cyclodextrins. A typical application of a Pirkle phase column was the use of a N-(3,5-dinitrobenzyl)-a-amino phosphonate to synthesize several functionalized chiral stationary phases to separate enantiomers of... [Pg.12]

The use of triphenylethylene SERMs as Pgp inhibitors for clinical application has been hampered by unacceptable toxicity at doses required to achieve adequate cellular concentration, which is likely due to the involvement of proteins with the ability to bind these compounds. For instance, toremifene is able to reverse MDR and to sensitize human renal cancer cells to vinblastine in vitro. However, in vivo toremifene is tightly bound to serum proteins, in particular a 1-acid glycoprotein (AAG), which may limit its tissue availability (Braybrooke et al. 2000). In agreement with this, Chatterjee and Harris (1990) have shown that tamoxifen and 4-OH-tamoxifen were similarly potent in reversing MDR in Chinese hamster ovary (CHO) cells with acquired resistance to adriamycin. However, the addition of AAG (0.5 to 2 mg/ml, the range found in vivo) to cell cultures decreased the effect of tamoxifen on reversing MDR, and at the highest AAG concentration there was a complete reversal of the effects of... [Pg.98]

The protein A (pA), antihuman serum albumin (a-HSA, M 150 kD), and human serum albumin (HSA, M 65 kD) were provided by Paradocs BV (Tiel, The Netherlands). The Herpes Simplex Virus type 1 (HSV-1) and anti-HSV-1 gG glycoprotein G monoclonal antibody (a-HSV-1 gG) were purchased from Virusys Corporation (Marriottsville, MD, USA). Bovine serum albumin (BSA, M 50 kD) was purchased from Sigma-Aldrich Chemie BV (Zwijndrecht, The Netherlands). Synthetic surface protein of Hepatitis-B virus generated in Hep-G2 cell-line (HEP G2, M 25 kD) was provided by BioMerieux BV (Boxtel, The Netherlands). Phosphate buffered saline (PBS) was used for all experiments. [Pg.283]

There have been several studies that underscore the importance of unbound concentration in cell-based studies of receptor function. In a model study of the effect of plasma protein binding on the renal transport of organic anions using the expression of various organic anion transporters (OATPs) in Xenopus oocytes, the transport of ochratoxin A, methotrexate, and estrone sulfate was found to be strongly inhibited by the addition of human serum albumin to the culture medium [16]. Similarly, the addition of oq-acid glycoprotein was found to reverse the blockade of sodium-ion current by cocaine in a preparation of cardiac myocytes [17]. [Pg.492]

L6. Laurell, A.-B., Influence of alpha-streptococci, pneumococci and Pasteurella pseudotuberculosis on human serum glycoproteins. Acta Pathol, et Microbiol. Scand. 47, 429 (1959). [Pg.184]


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See also in sourсe #XX -- [ Pg.21 ]




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