Proceedings of the National Academy of Sciences of the United States of America, 103(25), 9512-9517 (2006-06-14)
Natively unfolded phenylalanine-glycine (FG)-repeat domains are alleged to form the physical constituents of the selective barrier-gate in nuclear pore complexes during nucleocytoplasmic transport. Presently, the biophysical mechanism behind the selective gate remains speculative because of a lack of information regarding
Bioscience, biotechnology, and biochemistry, 71(8), 2083-2086 (2007-08-11)
The aim of this study was to improve the performance of affinity gels containing glycyl-D-phenylalanine (Gly-D-Phe) as a ligand to thermolysin. Gly-D-Phe was immobilized to the resin through spacers of varying chain lengths. The resulting affinity gels had spacer chain
The American journal of physiology, 260(3 Pt 2), R563-R569 (1991-03-01)
The transport mechanisms for the dipeptide glycyl-L-phenylalanine (Gly-Phe) and L-phenylalanine (Phe) were characterized in fish intestinal brush-border membrane vesicles (BBMV). Gly-Phe was rapidly hydrolyzed only intravesicularly with almost total hydrolysis occurring even at 10 s. Dipeptide uptake was not stimulated
Resolution of chiral compounds by HPLC using mobile phase additives and a porous graphitic carbon stationary phase.
B J Clark et al.
Journal of pharmaceutical and biomedical analysis, 7(12), 1883-1888 (1989-01-01)
Immobilisation of enzyme substrates is a powerful tool in the detection of enzymes in the chemosphere and the environment. A siloxane based strategy for the covalent immobilisation of oxidoreductase and protease substrates was developed involving activation of silica gel and
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