通过配体结合可以引起人体白蛋白血清的长效吸引潜力.docVIP

窗体顶端 窗体底端 窗体顶端 窗体底端 窗体顶端 窗体底端 窗体顶端 窗体底端 Dokumente DIMDI: MEDLINE (ME66) ? NLM ND: M PMID: STA: MEDLINE CED: DCO: Autoren: Sato T; Komatsu T; Nakagawa A; Tsuchida E Titel: Induced long-range attractive potentials of human serum albumin by ligand binding.通过配体结合可以引起人体白蛋白血清的长效吸引潜力 Quelle: Physical review letters; VOL:?98 (20); p.?208101 PM: Print-Electronic EPD: SU: IM Sprache: English CY: United States JID: 0401141 ISSN: 0031-9007 CO: PRLTAO Institution: Division of Pure and Applied Physics, Faculty of Science and Engineering, Waseda University, 3-4-1 Okubo, Shinjuku-ku, Tokyo 169-8555, Japan. takaaki.sato@waseda.jp DT: Journal Article; Research Support, Non-U.S. Govt Schlagw?rter CT: ELECTROSTATICS; HEME/*chemistry; HUMANS; RECOMBINANT PROTEINS/chemistry; SCATTERING, RADIATION; SERUM ALBUMIN/*chemistry; SPECTRUM ANALYSIS/methods; X-RAY DIFFRACTION/methods CTG: ELEKTROSTATIK; H?M/*Chemie; MENSCH; REKOMBINANTE PROTEINE/Chemie; STREUSTRAHLUNG; SERUMALBUMIN/*Chemie; SPEKTRALANALYSE/Methoden; R?NTGENBEUGUNG/Methoden TE: Recombinant Proteins; Serum Albumin; Heme/14875-96-8 CR: 14875-96-8 AB: Small-angle x-ray scattering and dielectric spectroscopy investigation on the solutions of recombinant human serum albumin and its heme hybrid revealed that heme incorporation induces a specific long-range attractive potential between protein molecules. This is evidenced by the enhanced forward intensity upon heme binding, despite no hindrance to rotatory Brownian motion, unbiased colloid osmotic pressure, and discontiguous nearest-neighbor distance, confirming monodispersity of the proteins. The heme-induced potential may play a trigger role in recognition of the ligand-filled human serum albumins in the circulatory system.对重组人体白蛋白血清和其杂种血红素小角度X线照射和电解质光谱学研究显示血红素结合引起蛋白分子之间一种特殊长效吸引潜力。这显示通过提高血红素结合强度，不管无障碍的回转Brownian动作、无偏向的胶体渗透压、和不连续的最近邻的距离，可以确定蛋白的单分散性。在循环系统中这种血红素引起的潜力可能有一种扳机作用来识别人体白蛋白血清的加载配体。 ? Volltext ? D