Chemical Characterization of Metal/Polymer interface

2015 ◽  
Vol 84 (8) ◽  
pp. 591-595 ◽  
Author(s):  
Yukiko IZUMI ◽  
Naoki BADEN ◽  
Kazuhiro MATSUDA
2018 ◽  
Vol 24 (1) ◽  
pp. 49-59 ◽  
Author(s):  
Marian C. Popescu ◽  
Bogdan I. Bita ◽  
Vasilica Tucureanu ◽  
Dan Vasilache ◽  
Melania A. Banu ◽  
...  

AbstractThe aim of this study is to conduct an extended surface and cross-section characterization of a denture base acrylic resin subjected to 500, 650, and 750 W microwave irradiation for 2, 3, and 5 min to assess its morphological modifications. A commercial heat-cured powder was polymerized according to the manufacturer’s specifications and distributed into 20 circular samples. A stainless-steel wire was partially embedded in half of the discs, in order to investigate the metal–polymer interface. High-resolution scanning electron microscopy (SEM) imaging, white light interferometry, roughness measurements and Fourier transform infrared spectrometry were employed for morphological and structural evaluation of the irradiated polymer. Superficial adaptation was discovered after 5 min exposure at 500 W, 650 W, and 750 W, revealing significant roughness correction for 750 W. SEM characterization revealed the inner alteration of the resin for the 750 W protocol and a metal–polymer gap developed regardless of the irradiation conditions. The considerable temperature fluctuations that the samples were subject to during the experiments did not essentially change the poly(methyl-methacrylate) bond structure.


1981 ◽  
Author(s):  
Birgitta Berglund ◽  
Ulf Berglund ◽  
Thomas Lindvall ◽  
Helene Nicander-Bredberg

1973 ◽  
Vol 74 (2) ◽  
pp. 226-236 ◽  
Author(s):  
Michel Chrétien ◽  
Claude Gilardeau

ABSTRACT A protein isolated from ovine pituitary glands has been purified, and its homogeneity assessed by NH2- and COOH-terminal amino acid determination, ultracentrifugation studies, and polyacrylamide gel electrophoresis after carboxymethylation. Its chemical and immunochemical properties are closely similar to those of beef and pork neurophysins, less similar to those of human neurophysins. It contains no tryptophan (like other neurophysins) or histidine (like all except bovine neurophysin-I and human neurophysins). It has alanine at the NH2-terminus and valine at the COOH-terminus. Its amino acid composition is similar to, but not identical with those of porcine and bovine neurophysins.


Alergologia ◽  
2020 ◽  
Vol 1 (4) ◽  
pp. 7
Author(s):  
Mariana Vieru ◽  
Florin-Dan Popescu ◽  
Laura Haidar ◽  
Carmen Bunu-Panaitescu

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