A proteomic map for human urine on two-dimensional (2-D) gels has been developed. Initial studies demonstrated that the urine proteins prepared by conventional methods showed interference and poor reproducibility in 2-D electrophoresis (2-DE). To address this issue, urine samples were dialyzed to remove any interfering molecules. The dialysis of urine proteins and the concentration by lyophilization without fractionation significantly improved the reproducibility and resolution and likely represents the total urine proteins on a 2-D gel. In addition, removing albumin from urine using Affi-Gel Blue helped to identify the low-abundant proteins. Using the developed method, we prepared proteins from urine collected from healthy females and males. The large inter- and intra-subject variation in protein profiles on 2-D gels made it difficult to establish a normal human urine proteomic 2-D map. To resolve this problem, urinary proteins were prepared from the pooled urine collected from 20 healthy females and males, respectively. The established male and female urine proteomes separated on 2-D gels were almost identical except for some potential sex-dependent protein spots. We have annotated 113 different proteins on the 2-D gel by peptide mass fingerprinting (PMF). We propose that the established total urine proteome can be used for 2-DE analysis, liquid chromatography-tandem mass spectrometry (LC-MS/MS), and identification of novel disease-specific biomarkers.

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The catalytic activities of tetraphenylporphinatoaluminum chloride (TPPAlCl) and its propylene oxide adduct (TPPAl(PO)2Cl) were investigated in detail together with a quarternary salt Et4NBr for the copolymerization of carbon dioxide and propylene oxide. In addition, for the components and starting raw materials of the catalyst systems, catalytic activities were examined for the copolymerization. The TPPAlCl catalyst delivered oligomers containing ether linkages to a large extent, regardless of its PO adduction. And cyclic propylene carbonate, as byproduct, was formed in a very small portion. Using the TPPAlCl coupled with Et4NBr as a catalyst system, the formation of ether linkages was reduced significantly in the copolymerization; however, the obtained oligomer still contained ether linkages of 25.0 mol % in the backbone. On the other hand, the formation of cyclic carbonate was increased to 22.4 mol % relative to the oligomer product. The results indicate that the salt, which was coupled with the TPPAlCl catalyst, plays a key role in reducing the formation of ether linkage in the oligomer and, however, in enhancing the formation of cyclic carbonate. Similar results were obtained for the copolymerization catalyzed by the TPPAl(PO)2Cl/Et4NBr system. That is, the formation of ether linkages was not restricted further by the PO adduction of the TPPAlCl component in the catalyst system. Only oligomers with a relatively high molecular weight were produced. This indicates that the PO adduction of the TPPAlCl component contributes highly to the initiation and propagation step in the oligomerization, consequently leading to a relatively high molecular weight oligomer. In contrast, the Et4NBr, as well as the Et2AlCl, produced only cyclic carbonate in a very low yield. Furthermore, tetraphenylporphine exhibited no catalytic activity, regardless of using together with Et4NBr. On the other hand, the Et2AlCl coupled with Et4NBr provided a low molecular weight oligomer having ether linkages of 92.3 mol % in addition to the cyclic carbonate. © 1999 John Wiley & Sons, Inc. J Polym Sci A: Polym Chem 37: 3329–3336, 1999

Triggering changes in surface porosity enabled the controlled release of biomolecules from elastin-like polypeptide (ELP) microspheres. The transition temperature (T(t)) of cross-linked microspheres was determined by differential scanning calorimetry, and T(t) was in agreement with the volume transition observed by changing the external temperature of the incubation media. The thermoresponsive pore structure of ELP microspheres and their surface morphology were examined by field-emission scanning electron microscopy. ELP microspheres were investigated as a smart drug carrier using model drug molecules, bovine serum albumin, and prednisone acetate. The release rate was accelerated by squeezing out the entrapped biomolecules as the temperature was increased above T(t) because of the development of micropores at the surface as well as in the bulk. In addition, the stepwise release confirmed that ELP microspheres could be progammed precisely to control the release of drugs by external stimuli.