Biomedical subjects

Yi Long

Publications and source records attributed to Yi Long.

3 recordsLinked to original sources

PubMed2006

Protein-imprinted polymer with immobilized assistant recognition polymer chains.

Here we introduce a new method for preparing a protein-imprinted polymer with immobilized assistant recognition polymer chains as an additional element of monomer to create effective recognition sites. In this work the bovine serum albumin was used as template and the template protein was selectively assembled with immobilized assistant recognition polymer chains from their library, numerous limited length polymer chains with randomly distributed recognition sites and immobilizing sites. These assemblies of protein and immobilized assistant recognition polymer chains would be adsorbed by the macro porous adsorbent spheres and immobilized by cross-linking polymerization. After removing the template, binding sites that were complementary to the target protein in size, shape and position of recognition groups were exposed, and their confirmation was preserved by the cross-linked structure. The synthesized imprinted polymer was used to adsorb BSA from protein mixtures, and showed a high selectivity.

Biocompatible Materials↗

PubMed2006

Molecular imprinted polymer with cloned bacterial protein template enriches authentic target in cell extract.

Here we describe a new method for preparing a protein-imprinted polymer with a cloned bacterial protein template, which recognizes/adsorbs authentic target protein present at a relatively low level in cell extract. In this work, cloned pig cyclophilin 18 (pCyP18) was used as a template. The template protein was selectively assembled with memory molecules from their library, which consists of numerous limited length polymer chains with randomly distributed recognition sites and immobilizing sites. These assemblies of protein and memory molecules were adsorbed by porous polymeric beads and immobilized by cross-linking polymerization. After removing the template, binding sites that were complementary to the target protein in size, shape and the position of recognition groups were exposed, and their confirmation was preserved by the cross-linked structure. The synthesized imprinted polymer was used to adsorb authentic pCyP18 from cell extract, and its proportional content was enriched 300 times.

Bacterial Proteins↗

PubMed2005

[Effect of caffeic acid, seopoletin and scutellarin on rat retinal neurons in vitro].

OBJECTIVE: To observe the effect of caffeic acid, seopoletin and scutellarin on rat retinal neurons in vitro and explore neuroprotection in glaucoma of Erigeron breviscapus. METHOD: The retinal of 18 post-natal 2-3 days Sprague-Dawley rats were dissociated into cell suspension with trypsin digestion. The cell suspension was implated in 96-well culture plates covered with hyaluronic acid and laminin in each well. After culturing for 3 days, caffeic acid, seopoletin and scutellarin were added to the cultures, continue to culture 2 days. Then, the A of living cells in each well was tested by MTT colorimetric microassay. Some of the 5-day culture cells were identified by Nissel technique. RESULT: Most of the living cells were retinal neurons by Nissel identification. The number of living cells increased significantly in high concentrations of caffeic acid, seopoletin and scutellarin compared with control group (P < 0.05, P < 0.01). CONCLUSION: caffeic acid, seopoletin and scutellarin can all promote retinal neurons to live in vitro, with caffeic acid being most effective.

Animals↗