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Average Molecular Mass (average + molecular_mass)
Selected AbstractsModification induced by alpha particle irradiationin Makrofol polycarbonateJOURNAL OF APPLIED POLYMER SCIENCE, Issue 6 2008S. A. Nouh Abstract Makrofol DE 1-1 CC polycarbonate samples were exposed to alpha particles of initial energies at levels between 5.1 and 34 MeV. The modifications induced in polycarbonate samples due to the alpha particle irradiation have been studied through different characterization techniques such as X-ray diffraction (XRD), infrared spectroscopy, intrinsic viscosity, and color difference studies. The infrared spectroscopy indicated that the intensities of the characteristic absorption bands decrease with increasing the deposited alpha energy in the range 5.1,8.4 MeV, indicating that the degradation is the dominant mechanism at this range. At the same time, an increase in the OH groups was observed at the same energy range 5.1,8.4 MeV due to the degradation of carbonate group and the H abstraction from the polymer backbone to form hydroxyl groups. The degradation reported by IR spectroscopy enhanced the degree of ordering in the degraded samples as revealed by XRD technique. Additionally, this degradation decreases the intrinsic viscosity from 0.56 to 0.43 at 35°C, indicating a decrease in the average molecular mass. The non irradiated Polycarbonate polymer is nearly colorless. It showed significant darkness sensitivity towards alpha particle irradiation, indicated by an increase in the color intercept L* from 33.6 to 36.7. © 2008 Wiley Periodicals, Inc. J Appl Polym Sci, 2008 [source] Thermosensitive Poly[(2-(diethylamino)ethyl methacrylate)- co -(N,N -dimethylacrylamide)] Cryogels Prepared by a Two-Step Polymerization MethodMACROMOLECULAR MATERIALS & ENGINEERING, Issue 10 2006Tuncer Caykara Abstract Summary: Temperature-sensitive P(DEAEMA- co -DMAAm) cryogels with five different DMAAm contents were synthesized via a two-step polymerization method, the initial polymerization being conducted for various times at 22,°C, followed by polymerization at ,26,°C for 24 h. The influence of the first-step time and the content of DMAAm on the swelling ratio and network parameters such as the polymer/solvent interaction parameter, the average molecular mass between crosslinks, and the mesh size of the cryogels were reported and discussed. The swelling studies indicated that the swelling increased in the following order: 22C45,>,22C30,>,22C15,>,22C0. The cryogels exhibited swelling/deswelling transitions (reentrant phenomena) in water depending on temperature. These properties were attributed to the macroporous and regularly arranged network of the cryogels. Scanning electron microscope graphs reveal that the macroporous network structure of the cryogels can be adjusted by applying a two-step polymerization. Chemical structure of the P(DEAEMA- co -DMAAm) cryogels. [source] Analytical characterization of PEG polymers by MEKCELECTROPHORESIS, Issue 4 2010Marķa R. Plata Abstract Characterization of PEGs with average molecular masses of up to 2000 has been achieved using MEKC with UV detection. A rapid derivatization procedure with phenyl isocyanate using microwave radiation, in order to introduce chromophore groups in PEGs, has been developed involving a reaction time of 60,s. Different optimized conditions in accordance with the molecular weight have been studied to obtain the oligomer separation. The weight-average molecular mass the number-average molecular mass and the degree of polydispersity (molecular mass distribution) were calculated for the different PEGs obtaining similar results with those certified for standards. A good precision was obtained for characterizing the different oligomers. Ethylene glycol was used as the internal standard for the analysis of low-molecular-weight PEGs. The developed method was satisfactorily applied to the characterization of these polymers in several real samples, such as lubricant eye drops, toothpaste, tap water and eye make-up remover. [source] Molecular mass determination of plasma-derived glycoproteins by ultraviolet matrix-assisted laser desorption/ionization time-of-flight mass spectrometry with internal calibrationJOURNAL OF MASS SPECTROMETRY (INCORP BIOLOGICAL MASS SPECTROMETRY), Issue 11 2002Omar Belgacem Abstract Human plasma-derived antithrombin III (AT-III), factor IX (FIX) and vitronectin (VN) were characterized as native glycoproteins and in their de- N -glycosylated form by means of MALDI mass spectrometry. The average molecular masses of the three complex glycoproteins were determined applying internal calibration with high-mass, well-defined protein calibrants. Internal calibration generated for the 47 kDa yeast protein enolase a mass precision in the continuous and delayed extraction mode of ±0.12 and ±0.022%, respectively. The achievable mass accuracy for such a high-mass, unmodified protein was in the range of 0.02% in the continuous mode, which turned out to be better than in the delayed extraction mode. Purification of all (glyco) proteins (even the calibration proteins) by means of ZipTip® technology and direct elution with a solvent system containing the appropriate MALDI matrix turned out to be a prerequisite to measure the exact molecular masses with an internal calibration. The average molecular masses of the two different forms of AT-III, namely AT-III, and AT-III,, were shown to be 57.26 and 55.04 kDa, respectively. The 2.22 kDa mass difference is attributed to the known difference in carbohydrate content at one specific site (Asn-135). After exhaustive de- N -glycosylation (by means of PNGase F) of the ,- and ,-form and subsequent MALDI-MS analysis, average molecular masses of 48.96 and 48.97 kDa, respectively, were obtained. These values are in good agreement (,0.15%) with the calculated molecular mass (49.039 kDa) of the protein part based on SwissProt data. The molecular mass of the heavily post-translational modified glycoprotein FIX was found to be 53.75 kDa with a peak width at 10% peak height of 4.5 kDa, because of the presence of many different posttranslational modifications (N - and O -glycosylation at multiple sites, sulfation, phosphorylation, hydroxylation and numerous ,-carboxyglutamic acids). MALDI-MS molecular mass determination of the native, size-exclusion chromatography-purified, VN sample revealed that the glycoprotein was present as dimer with molecular mass of 117.74 kDa, which could be corroborated by non-reducing SDS-PAGE. After sample treatment with guanidine hydrochloride and mass spectrometric analysis, a single, new main component was detected. The molecular mass turned out to be 59.45 kDa, representing the monomeric form of VN, known as V75. The determined molecular mass value was shown to be on one hand lower than from SDS-PAGE and on the other higher than the calculated amino acid sequence molecular mass (52 277 Da), pointing to the well-known SDS-PAGE bias and to considerable post-translational modifications. Further treatment of the sample with a reducing agent and subsequent MALDI-MS revealed two new components with molecular masses of 49.85 and 9.41 kDa, corresponding to V65 and V10 subunits of VN. PNGase F digest of the V75 and V65 units and MS analysis, exhibiting a molecular mass reduction of 6.37 kDa in both cases, verified the presence of a considerable amount of N -glycans. Copyright © 2002 John Wiley & Sons, Ltd. [source] | ||||||||||