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Protein adsorption studies

Golander C G, Lin Y S, Fllady V and Andrade J D 1990 Wetting and plasma-protein adsorption studies using surfaoes with a hydrophobieity gradient Colloids Surf. 49 289-302... [Pg.2639]

Tengvall P, Lundstrom I, Liedberg B (1998) Protein adsorption studies on model organic surfaces an ellipsometric and infrared spectroscopic approach. Biomaterials 19 407-422... [Pg.194]

Protein adsorption studies are performed either on high surface area material dispersed in a liquid phase containing dissolved protein, or on low surface area material, often flat, which is in contact with protein solution. Both approaches complement each other and can provide valuable information about adsorbed protein layers. [Pg.47]

The major advantage of protein adsorption studies on high surface area materials is that changes of some extensive properties which accompany the process of adsorption are large enough to be directly measured heat of adsorption through microcalorimetry 141), uptake or release of small ions by a combination of electrokinetic methods and titration 142), thickness of adsorbed layer or an increase of the volume fraction of solid phase by a hydrodynamic method like viscometry 143). Chromatographiclike analysis can also be applied to protein adsorption 144). [Pg.48]

ATR spectroscopy in the infrared has been used extensively in protein adsorption studies. Transmission IR spectra of a protein contain a wealth of conformational information. ATR-IR spectroscopy has been used to study protein adsorption from whole, flowing blood ex vivo 164). Fourier transform (FT) infrared spectra (ATR-FTIR) can be collected each 5-10 seconds165), thus making kinetic study of protein adsorption by IR possible 166). Interaction of protein with soft contact lens materials has been studied by ATR-FTIR 167). The ATR-IR method suffers from problems similar to TIRF there is no direct quantitation of the amount of protein adsorbed, although a scheme similar to the one used for intrinsic TIRF has been proposed 168) the depth of penetration is usually much larger than in any other evanescent method, i.e. up to 1000 nm water absorbs strongly in the infrared and can overwhelm the protein signal, even with spectral subtraction applied. [Pg.52]

QCM has been used extensively in the areas of DNA hybridization, protein adsorption studies, immunological systems and also in the areas of protein-protein and protein-carbohydrate interaction [24]. Examples prepared using carbohydrate SAMs to function as lectin biosensors are known since initially it was shown... [Pg.144]

Infrared spectra of proteins may be obtained either in the solid state (KBr pellets, crystals, or by diffuse reflectance techniques (Yang et al., 1985)) or in solution (D2O solutions, ATR techniques, as in the case of protein adsorption studies (Gendreau et al., 1982 Sec. 6.4). Raman spectra of proteins are usually obtained in solution. [Pg.356]

The Effect of Monomer Purity on Protein Adsorption onto Poly-(HEMA). The importance of relatively minor contamination of the monomers used in formulating hydrogels to be used in biomedical applications has not been recognized widely as yet, although Bruck has referred to this problem in connection with the soft contact lens (26). Protein adsorption studies performed with hydrogels made with monomers of typical commercial quality illustrate this potential problem. [Pg.234]

Golander, C.-G. Lin, Y.-S. Hlady, V. Andrade, J. D., Wetting and plasma-protein adsorption studies using surfaces with a hydrophobicity gradient, Colloid Surf. 1990, 49, 289-302... [Pg.77]

In vitro protein adsorption studies are relevant to in vivo behavior in humans. [Pg.13]

The protein adsorption studies described in this volume provide a representative cross section of the current research in this area. The compositional and structural aspects of proteins at interfaces continue to receive major attention. Both new and previously developed techniques are being applied to these problems. [Pg.238]

Protein adsorption studies were done by immersing polymer discs for 24 h in room-temperature solutions of radiolabeled gamma-globulin, albumin, and lysozyme. Standard scintillation counting methods were used to quantify the amount of protein bound to the polymer surfaces after a thorough rinse with physiological saline solution (0.9% aqueous NaCl). [Pg.64]

The reference list includes all publications from my laboratory that have involved or been closely related to protein adsorption studies (1-29). These publications and their principal results are summarized and listed in Table 1 in their order of appearance in the literature, which approximates the sequence in which they were actually done. Portions of this work have already been reviewed in more detail elsewhere (26.27). In what follows, certain aspects of the methods, results, and conclusions of these studies are discussed. [Pg.240]

This paper is a detailed presentation of the techniques used in my lab for protein adsorption studies. [Pg.254]

The protein adsorption studies described were all at the liquid - solid or solid - air interface. Lateral scanning elllpsometry was made to evaluate the surfaces with a wettability gradient. Experiments were most often made on (modified) silicon surfaces. The experimental results are also discussed in relation to the proposed theoretical models for protein adsorption. [Pg.468]

Protein diffusivity, however, is not always the main determinant in the composition of adsorbed protein layers. If this were the case, the composition of the adsorbed protein layer would be the same on different materials exposed to the same solution. This condition is not usually observed (Horbett, 1999), indicating that the affinity of each protein is influenced by the surface chemistry of the biomaterial (Horbett and Brash, 1995). Because proteins differ in affinity for various surface chemistries, the competitive protein adsorption process will also differ, leading to unique protein layer compositions upon different materials. Furthermore, the vast majority of protein adsorption studies have been carried out in vitro, assuming that this accurately mimics the in vivo environment. However, differences in implant site (i.e., blood-contacting devices vs solid tissue... [Pg.27]

Ekici S (2011) Intelligent poly(A-isopropylacrylamide)-carboxymethyl cellulose full interpenetrating polymeric networks for protein adsorption studies. J Mater Sd 46 2843-2850... [Pg.249]

We would like to express thanks to our co-workers, especially Mr. K. Birkner for the sputtering work. Dr. G. Hellwig for protein adsorption studies. Dr. B. Schindler for developing plasma deposition, and Mr. N. Stroh and Mr. M. Timmermann for filtration experiments. We are grateful to Dr. Lemm, Ber-for competitive adsorption measurements. [Pg.308]

TABLE 2 Characteristics of the Surfaces Used for the Protein Adsorption Study Surface Density of PEG Chains, PEG, and of Free Amine Groups in PLL, n (free), and... [Pg.303]

Protein adsorption studies on artificial hip-joint materials have focused mainly on albumin, as this is the most abundant protein in synovial fluid. Studies to evaluate albumin adsorption on ceramics and metals have been carried out using XPS and radiolabeling techniques [10.11] as well as sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and chromatography [12,13]. Fluorescence microscopy has been applied to evaluate albumin adsorption on UHMWPE [6,14]. [Pg.405]


See other pages where Protein adsorption studies is mentioned: [Pg.182]    [Pg.348]    [Pg.348]    [Pg.117]    [Pg.146]    [Pg.37]    [Pg.51]    [Pg.52]    [Pg.241]    [Pg.68]    [Pg.65]    [Pg.67]    [Pg.127]    [Pg.66]    [Pg.254]    [Pg.613]    [Pg.376]    [Pg.192]    [Pg.182]    [Pg.289]    [Pg.478]    [Pg.497]    [Pg.526]    [Pg.553]    [Pg.791]    [Pg.162]   
See also in sourсe #XX -- [ Pg.15 , Pg.16 ]

See also in sourсe #XX -- [ Pg.30 , Pg.31 ]




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