Restriction Enzyme Database

REBASE-The Restriction Enzyme Database Restriction enzyme directory and action http //rebase. neb.com/... 

INTERNET LINK REBASE, The Restriction Enzyme Database... 

Gene sequence database. More than 20 other databases including SWISS-PROT, ACeDB, FlyBase, Eukaryotic Promoter Database, Restriction Enzyme Database, Transcription Factor Database, and CarbBank/CCSD. Databases and software development tools for sequence data available for anonymous ftp ncbi.nlm.nih.gov (130.14.25.1). 

The classic enzyme commission (EC) classification for GTs is on the basis of their donor and acceptor specihcity as well as the product formed. Currently, 295 entries are in this database (http //www.chem.qmul.ac.uk/iubmb/). The distinction between these enzymes is noted by their ability to catalyze the transfer of hexoses (EC 2.4.l.y, hexosyltransferases), pentoses (EC 2.4.2.y, pentosyltransferases), or other glycosyl groups (2.4.99.y, sialyltransferases). This classification is restricted to enzymes that are fully characterized, and it can be problematic for enzymes that act on several distinct acceptors but at different rates. It also does not take into account the origin of the enzyme or its three-dimensional stmcture. 

Roberts RJ, Vincze T, Posfai J, Macelis D (2010) REBASE—a database for DNA restriction and modification enzymes, genes and genomes. Nucleic Acids Res 38(Database issue) D234-D2 3 6... 

Roberts, R. J., and D. Macelis. 1997. REBASE—restriction en-Z3unes and methylases. Nucl. Acids Res. 25 248-262. Information on accessing a continuously updated database on restriction and modification enzymes at http //www.neb.com/rebase. 

Protein arrays with 10-500 antibodies printed onto an array use detection techniques, including fluorescence and multiple sandwich enzyme-linked immunosorbent assays, but the broad application of these assays is restricted by lack of suitable antibodies for laboratory animals and some potential cross-reactivities between antibodies with similar affinities. Calibration, reproducibility, and identification of proteins are common problems for all of these technologies. A number of databases are available to help investigators identify the numerous proteins found using these separation techniques, particularly for mass spectrometer data. 

In principle, any method intended for protein fractionation can be used for enzyme purification. However, the methods applicable for production purposes are restricted to those amenable for scale-up at a reasonable cost. Only those will be reviewed here. Comprehensive reviews on protein purification can be found elsewhere (Asenjo 1990 Janson and Ryd6n 1998 Roe 2001 Hatti-Kaul and Mat-tiasson 2003b Rosenberg 2004) and handbooks on the subject are also available (http //www.biochem.uiowa.edu/donelson/Database%20items/protein purification handbook.pdf). 

Loureiro, 2000 Deak, 2002 Capece et al., 2003). Each requires initial digestion of the harvested DNA using restriction endonucleases, enzymes that cleave DNA at specific nucleotide sequences unique for that enzyme. The DNA digest is the amplified at specific or randomly selected regions by polymerase chain reaction (PCR). Fragments are subsequently separated electrophoretically and their patterns compared against those of other isolates or databases. 

The requirement of good biocompatibility and partitioning behavior of substrate and product are restrictive criteria for the selection of a suitable solvent. Many attempts have been made to correlate the toxicity of different solvents to their physicochemical properties. Laane et al. first addressed this issue in a comprehensive fashion and pointed out that the logarithm of the partition coefficient, logP, as an indicator of solvent hydrophobicity, correlates best with enzyme activity [14]. The product recovery capacity and selectivity are quantified by the partition coefficient and the separation factor whose accurate values can only be obtained experimentally, but preliminary screening can be done with established databases [15]. 

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