Detail of "73768-94-2"

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Measuring reaction rate coefficient in analysis utilizing surface plasmon resonance, and biochemical applications

All Rights Reserved. Measuring reaction rate coefficient in analysis utilizing surface plasmon resonance, and biochemical applications. Some, Masato (Fuji Photo Film Co., Ltd., Japan). U.S. Pat. Appl. Publ. US 2007031893 A1 8 Feb 2007, 15pp. (English). (United States of America). CODEN: USXXCO. INCL: 435007100; 702019000; 702022000. APPLICATION: US 2006-496483 1 Aug 2006. PRIORITY: JP 2005-222953 1 Aug 2005. DOCUMENT TYPE: Patent CA Section: 9 (Biochemical Methods) Section cross-reference(s): 67 An object of the present invention is to provide a method for measuring a reaction rate coeff. in an anal. utilizing total reflection attenuation, which is capable of calcg. the reaction rate coeff. speedily and accurately. The present invention provides a method for measuring adsorption rate coeff. (Ka) and diffusion coeff. (D) in a reaction between an analyte mol. immobilized on a metal surface and a mol. that interacts with the analyte mol., by measuring an angular change in the total reflection attenuation angle (qSP) using an anal. device utilizing total reflection attenuation, preferably a surface plasmon resonance device. The method of the invention comprises: (1) providing multiple simulation curves of a binding dissocn. reaction for sets of variables in which Ka and D are each varied within a predetd. 9004-54-0 and 73768-94-2 which are cas registry numbers of chemicals are mentioned. width; (2) prepg. a measurement curve of the binding dissocn. reaction based on an angular change in a measured total reflection attenuation angle (qSP); (3) examg. the level of correspondence between the measurement curve prepd. in (2) and the multiple simulation curves of (1), and (4) applying the Ka and D that were used for the prepn. of the simulation curve with the highest level of correspondence to the Ka and D in the reaction between the analyte mol. immobilized on the metal surface and the mol. that interacts with the analyte mol. Exemplary prepn. of a biochip having protein A immobilized thereon and evaluation of binding performance of mouse IgG is described. .

The effect of surface chemistry on the formation of thin films of native fibrillar collagen

All Rights Reserved. The effect of surface chemistry on the formation of thin films of native fibrillar collagen. Elliott, John T.; Woodward, John T.; Umarji, Anita; Mei, Ying; Tona, Alessandro (Biochemical Science Division, Chemical Science and Technology Laboratory, National Institute of Standards and Technology, Gaithersburg, MD 20899, USA). Biomaterials, Volume Date 2007, 28(4), 576-585 (English) 2006 Elsevier Ltd. CODEN: BIMADU. ISSN: 0142-9612. DOCUMENT TYPE: Journal CA Section: 63 (Pharmaceuticals) In this study, we used well-defined, homogeneous, gradient and patterned substrates to explore the effects of surface chem. on the supramol. structure of adsorbed type I collagen. Type I collagen (320 mg/mL) was allowed to adsorb onto self-assembled CH3- COOH-, NH2- and OH-terminated alkylthiolate monolayers at 37°. At. force microscopy, ellipsometry and phase microscopy indicated that large supramol. collagen fibril structures (approx. 200 nm in diam., several microns long) assembled only at the hydrophobic CH3- terminated surfaces. By varying the surface energy using a mixt.Several substances with their cas registry numbers 69839-68-5 and 73768-94-2 may be metioned in this study. of OH- and CH3- terminated thiols during monolayer formation, we found that large fibril assembly occurred at surfaces with a water contact angle above 83°, but not on surfaces with a water contact angle below 63°. Examg. a surface with a linear hydrophobicity gradient revealed that the assembly of large collagen fibrils requires a hydrophobic surface with a water contact angle of at least 78°. Collagen fibril d. increased over a narrow range of surface energy and reached near-max. d. on surfaces with a water contact angle of 87°. These studies confirm that the supramol. structure of adsorbed collagen is highly dependent on the underlying substrate surface chem. We can take advantage of this dependency to pattern areas of fibrillar and non-fibrillar collagen on a single surface. Morphol. studies with vascular smooth muscle cells indicated that only collagen films formed on hydrophobic substrates mimicked the biol. properties of fibrillar collagen gels. .