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10.1007/s10867-015-9379-y http://scihub22266oqcxt.onion/10.1007/s10867-015-9379-y C4456488!4456488!25764184     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Biol+Phys 2015 ; 41 (3): 293-301 Nephropedia Template TP {{tp|p=25764184|t=2015. Far-infrared spectroscopy of salt penetration into a collagen fiber scaffold |pdf=|usr=}}{{25764184}} gab.com Text Far-infrared spectroscopy of salt penetration into a collagen fiber scaffold JO: J Biol Phys http://www.kidney.de/pget.php?&tw=1&pmid=25764184 #FOAvip We employed far-infrared spectroscopy to observe the amount of salt that penetrates into collagen fiber masses. The absorption properties of collagen sheets prepared from tilapia skin, bovine skin, rat tail, and sea cucumber dermis were measured using a transmission Fourier transform spectrometer in a band from approximately 100 to 700 cm?1. We confirmed that the absorbance spectra of the four types of dried collagen sheet show good agreement, even though the amino acid compositions differed. The absorbance peaks observed in the band corresponded to collective vibrations of plural functional groups such as methylene and imino groups in collagen. When salt solution was added to the collagen sheets and then dried, the spectral shapes of the sheets at approximately 166 cm?1 were clearly different from those of the plain collagen sheets. The differential absorbance between wavenumbers 166 cm?1 and 250 cm?1 sensitively reflected the difference between higher-order structures, and the salt diffusion (crystallization) depended on the collagen fiber condition. From these results, we consider that spectral changes can be used for the numerical evaluation of salt penetration into a collagen fiber scaffold. Twit Text FOAVip Far-infrared spectroscopy of salt penetration into a collagen fiber scaffold ????J Biol Phys http://www.kidney.de/pget.php?&tw=1&pmid=25764184 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25764184 #FOAvip English Wikipedia <ref>{{Cite pmid|25764184}}</ref> Far-infrared spectroscopy of salt penetration into a collagen fiber scaffold #MMPMID25764184 Mizuno M; Yamada A; Fukunaga K; Kojima H J Biol Phys 2015[Jun]; 41 (3): 293-301 PMID25764184show ga We employed far-infrared spectroscopy to observe the amount of salt that penetrates into collagen fiber masses. The absorption properties of collagen sheets prepared from tilapia skin, bovine skin, rat tail, and sea cucumber dermis were measured using a transmission Fourier transform spectrometer in a band from approximately 100 to 700 cm?1. We confirmed that the absorbance spectra of the four types of dried collagen sheet show good agreement, even though the amino acid compositions differed. The absorbance peaks observed in the band corresponded to collective vibrations of plural functional groups such as methylene and imino groups in collagen. When salt solution was added to the collagen sheets and then dried, the spectral shapes of the sheets at approximately 166 cm?1 were clearly different from those of the plain collagen sheets. The differential absorbance between wavenumbers 166 cm?1 and 250 cm?1 sensitively reflected the difference between higher-order structures, and the salt diffusion (crystallization) depended on the collagen fiber condition. From these results, we consider that spectral changes can be used for the numerical evaluation of salt penetration into a collagen fiber scaffold. äFar-infrared spectroscopy of salt penetration into a collagen fiber sc(epmc).pdf DeepDyve Pubget Overpricing