Quantitative surface studies of protein adsorption by infrared spectroscopy: II. Quantification of adsorbed and bulk proteins
β Scribed by David J. Fink; Tim B. Hutson; Krishnan K. Chittur; R.Michael Gendreau
- Publisher
- Elsevier Science
- Year
- 1987
- Tongue
- English
- Weight
- 707 KB
- Volume
- 165
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
β¦ Synopsis
Attenuated total reflectance Fourier transform infrared spectra of surface-adsorbed proteins are correlated with concentration measurements determined by 125I-labeled proteins. This paper demonstrates that linear correlations between the intensity of the major bands of proteins and the quantity of proteins can be obtained for human albumin and immunoglobulin G up to surface concentrations of approximately 0.25 microgram/cm2. A poorer correlation was observed for human fibrinogen. A linear correlation was also observed between the concentration in the bulk solution and the major bands of albumin up to a concentration of 60 mg/ml.
π SIMILAR VOLUMES
Objectives: To determine the feasibility of near-infrared analysis for quantitating urea, creatinine, and protein in urine. Practical advantages of this method include ease of sample presentation and the absence of reagents or disposables. Design and Methods: The near-infrared methods were develope
## Abstract The adsorption of blood proteins onto various surfaces in contact with __flowing__ blood plasma or serum has been investigated using Fourier Transform infrared spectroscopy (FTβIR) coupled with attenuated total reflection (ATR). Comparison of adsorption from a static versus a flowing bl
FT-IR/PAS (Fourier transform infrared/photoacoustic spectroscopy) was used to evaluate the secondary structure of proteins. Four well-studied proteins, concanavalin A, hemoglobin, lysozyme, and trypsin, which have different distributions of secondary structures, were used for assignments of the infr
The adsorption of protein A on silicon surfaces was studied by atomic force microscopy (AFM) and X-ray photoelectron spectroscopy. The deposition was made statically from various concentrations of protein A in water solution. The biological activity was checked by the immobilization of rabbit immuno