Biomaterial Database

Protein recognition via molecularly imprinted agarose gel membrane. 2008

Yuan Lin, and Shunqing Tang, and Xuan Mao, and Lei Bao

Institute of Biomedical Engineering, Jinan University, Guangzhou 510632, People's Republic of China.

Agarose gel membranes (AGMs), which could selectively recognize bovine serum albumin (BSA) and bovine hemoglobin (Hb), were prepared by molecular imprinting technique under moderate preparation conditions. Four imprinting processes, including gelation without any treatment, second gel-melting, and two glutaraldehyde crosslinking processes of fumigation or direct addition of the crosslinking agent, were developed to investigate the protein-recognition behavior of the AGMs. Results showed that the preparation processes affected the adsorption capacity and selectivity of the imprinted AGMs. Both BSA- and Hb-imprinted AGMs exhibited higher adsorption abilities for the targeted proteins (3.77-5.72 times for BSA, 1.31-2.18 times for Hb) than the nonimprinted ones. And the selectivity of BSA-imprinted AGMs for BSA molecules (the selective factor K = 3.29-4.90) was higher than that of Hb-imprinted AGMs for Hb (K = 0.32-1.17). The optimal adsorption capacity of BSA- and Hb-imprinted AGMs was 25.90 and 117.45 mg/g, respectively, when the membrane was crosslinked by glutaraldehyde with a fumigation process; the optimal selectivity of BSA- and Hb-imprinted AGMs was 4.91 when the membrane was prepared by second gel-melting process, and 0.76 when the membrane was prepared without any treatment. These findings demonstrate that the molecularly imprinted AGMs are hopeful to be used in specific protein analysis.

UI	MeSH Term	Description	Entries
D008567	Membranes, Artificial	Artificially produced membranes, such as semipermeable membranes used in artificial kidney dialysis (RENAL DIALYSIS), monomolecular and bimolecular membranes used as models to simulate biological CELL MEMBRANES. These membranes are also used in the process of GUIDED TISSUE REGENERATION.	Artificial Membranes,Artificial Membrane,Membrane, Artificial
D011506	Proteins	Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.	Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene
D002417	Cattle	Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.	Beef Cow,Bos grunniens,Bos indicus,Bos indicus Cattle,Bos taurus,Cow,Cow, Domestic,Dairy Cow,Holstein Cow,Indicine Cattle,Taurine Cattle,Taurus Cattle,Yak,Zebu,Beef Cows,Bos indicus Cattles,Cattle, Bos indicus,Cattle, Indicine,Cattle, Taurine,Cattle, Taurus,Cattles, Bos indicus,Cattles, Indicine,Cattles, Taurine,Cattles, Taurus,Cow, Beef,Cow, Dairy,Cow, Holstein,Cows,Dairy Cows,Domestic Cow,Domestic Cows,Indicine Cattles,Taurine Cattles,Taurus Cattles,Yaks,Zebus
D003432	Cross-Linking Reagents	Reagents with two reactive groups, usually at opposite ends of the molecule, that are capable of reacting with and thereby forming bridges between side chains of amino acids in proteins; the locations of naturally reactive areas within proteins can thereby be identified; may also be used for other macromolecules, like glycoproteins, nucleic acids, or other.	Bifunctional Reagent,Bifunctional Reagents,Cross Linking Reagent,Crosslinking Reagent,Cross Linking Reagents,Crosslinking Reagents,Linking Reagent, Cross,Linking Reagents, Cross,Reagent, Bifunctional,Reagent, Cross Linking,Reagent, Crosslinking,Reagents, Bifunctional,Reagents, Cross Linking,Reagents, Cross-Linking,Reagents, Crosslinking
D005976	Glutaral	One of the protein CROSS-LINKING REAGENTS that is used as a disinfectant for sterilization of heat-sensitive equipment and as a laboratory reagent, especially as a fixative.	Glutaraldehyde,Cidex,Diswart,Gludesin,Glutardialdehyde,Glutarol,Korsolex,Novaruca,Sekumatic,Sonacide,Sporicidin
D006454	Hemoglobins	The oxygen-carrying proteins of ERYTHROCYTES. They are found in all vertebrates and some invertebrates. The number of globin subunits in the hemoglobin quaternary structure differs between species. Structures range from monomeric to a variety of multimeric arrangements.	Eryhem,Ferrous Hemoglobin,Hemoglobin,Hemoglobin, Ferrous
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D012685	Sepharose		Agarose,Sepharose 4B,Sepharose C1 4B,4B, Sepharose C1,C1 4B, Sepharose
D012710	Serum Albumin, Bovine	Serum albumin from cows, commonly used in in vitro biological studies. (From Stedman, 25th ed)	Fetal Bovine Serum,Fetal Calf Serum,Albumin Bovine,Bovine Albumin,Bovine Serum Albumin,Albumin, Bovine,Albumin, Bovine Serum,Bovine Serum, Fetal,Bovine, Albumin,Calf Serum, Fetal,Serum, Fetal Bovine,Serum, Fetal Calf
D054802	Molecular Imprinting	A methodology for chemically synthesizing polymer molds of specific molecules or recognition sites of specific molecules. Applications for MOLECULARLY IMPRINTED POLYMERS (MIPs) include separations, assays and biosensors, and catalysis.	Molecular Imprinting Technique,Imprinting, Molecular,Imprinting Technique, Molecular,Imprinting Techniques, Molecular,Molecular Imprinting Techniques,Technique, Molecular Imprinting,Techniques, Molecular Imprinting