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Myoglobin sample preparation

Figure 2.9. Schematic of a matrix-assisted laser desorption/ionization (MALDI) event. The SEM micrograph depicts sinapinic acid-equine myoglobin crystal from a sample prepared according to the dried drop sample preparation method. In the desorption event neutral matrix molecules (M), positive matrix ions (M+), negative matrix ions (M-), neutral analyte molecules (N), positive analyte ions (+), and negative analyte ions (-) are created and/or transferred to the gas phase. Reprinted from A. Westman-Brinkmalm and G. Brinkmalm (2002). In Mass Spectrometry and Hyphenated Techniques in Neuropeptide Research, J. Silberring and R. Ekman (eds.) New York John Wiley Sons, 47-105. With permission of John Wiley Sons, Inc. Figure 2.9. Schematic of a matrix-assisted laser desorption/ionization (MALDI) event. The SEM micrograph depicts sinapinic acid-equine myoglobin crystal from a sample prepared according to the dried drop sample preparation method. In the desorption event neutral matrix molecules (M), positive matrix ions (M+), negative matrix ions (M-), neutral analyte molecules (N), positive analyte ions (+), and negative analyte ions (-) are created and/or transferred to the gas phase. Reprinted from A. Westman-Brinkmalm and G. Brinkmalm (2002). In Mass Spectrometry and Hyphenated Techniques in Neuropeptide Research, J. Silberring and R. Ekman (eds.) New York John Wiley Sons, 47-105. With permission of John Wiley Sons, Inc.
Holo form of myoglobin analyzed. Sample preparation denatures the protein so the noncovalent heme group (616 Da) is lost and the observed mass is for apo-myoglobin. Spectra consist primarily of [M + H] ions. Ions with h her charge states, usually [M + 2H], have low intensities. Accuracy of mass determination for proteins is +0.1%. Resolution is Umited therefore, peaks are relatively broad. [Pg.69]

Meat discoloration studies typically involve a maximum of 5 days, with discoloration analy-sis being performed every day or on alternate days. The actual experimental time involved in the objective assessment of discoloration is not extensive and depends on the number of samples being analyzed. Colorimetric measurements with hand-held colorimeters are very rapid (three measurements per meat surface in < 1 min). Spectral scans of meat surfaces require 1 to 2 min. Extraction and analysis of ground meat products has the added step of homogenization and filtration prior to spectrophotometry, but relative to many laboratory procedures, this is relatively quick. Isolation and purification of preparative amounts of myoglobin requires only 2 to 3 days once appropriate preparations are made. Finally, metmyoglobin can be reduced to oxymyoglobin in 15 to 20 min. [Pg.918]

The solutions were prepared at a concentration of 200mg/ml by dissolving sperm whale myoglobin (Miles Laboratories (PTY) Limited) in de-ionised water. The samples were electro-dialysed before measurement to reduce the ionic conductivity. [Pg.58]

The mechanism of CO-release is unknown. In pure water, CO release is very slow but in the presence of myoglobin it is very rapid with ti/2 < 2 min. When dissolved in phosphate buffer for 24 h, [Ru(CO)3Cl(glycinate)] is deactivated and no longer releases CO. This combination of properties makes [Ru(CO)3C1 (glycinate)] ideal for use as a CO-RM. Solutions can be prepared and administered without significant loss of CO, and then release CO after administration. [Ru (CO)3Cl(glycinate)] deactivated with phosphate buffer provides a reference sample which does not release CO so that the effects of CO can be investigated. [Pg.259]

Accuracy in MS depends on calibration of the mlz axis of the spectra. Calibration is typically performed using separate samples or solutions of the calibrant studied under identical instrumental conditions as the analyte. Calibrants are selected based on the ionization technique and the mlz range required for the analyte typical calibrants used for soft ionization methods with biomolecules include bovine trypsin fragments, bovine insulin (5734 Da), cytochrome c (12,361 Da), horse myoglobin (16,951 Da), lysozyme (14,317 Da), and propylene glycols. Separate solutions of the analyte prepared in the absence and presence of a calibrant species may also be used. Table 15.6 shows typical calibration peaks found with bovine trypsin autolysis fragments.15... [Pg.308]

Fig. 7. Experimental Mossbauer spectra of frozen solution of MbCO. (a) T = 4.2 °K Ho = 0. (b) T = 4.2°K, Ho = 47 kOe, Ho L y. The additional resonances at —0.9 mm/sec and +1.33 mm/sec are due to oxygenated myoglobin (MbCC>2) which remained in the sample through the preparation of MbCO. The broad shoulders in (b) are probably due to the impurity effect of MbOg. [Taken from Ref. (50)]... Fig. 7. Experimental Mossbauer spectra of frozen solution of MbCO. (a) T = 4.2 °K Ho = 0. (b) T = 4.2°K, Ho = 47 kOe, Ho L y. The additional resonances at —0.9 mm/sec and +1.33 mm/sec are due to oxygenated myoglobin (MbCC>2) which remained in the sample through the preparation of MbCO. The broad shoulders in (b) are probably due to the impurity effect of MbOg. [Taken from Ref. (50)]...
Space for the monolithic column. The wall modification and preparation of the polyfethylhexyl methacrylate-co-ethylene dimethacrylate) monolith was identical with that shown earlier. The ultimate test of the performance of the system included separation of a digest of three proteins— BSA, myoglobin, and cytochrome c. The sequence coverage obtained using the microchip with two monolithic columns run in parallel is shown in Table 47.1 and compared with MALDI-MS analysis data obtained for nonfractionated sample. Clearly, the separation on chip containing monolith affords significantly better results. [Pg.1306]

As with any analytical method, the success of the bioassay is highly dependent on how the samples are collected and prepared. Care must be taken during all of the steps of the analysis to ensure that oxygen is not allowed to bind with myoglobin and that all measurements are carried out very carefully. Furthermore, attention to sample acquisition must be taken to ensure that small gas bubbles are not entrained in the samples when they are collected as this leads to errors (Kapic, 2005). Although difficult to use, the bioassay technique, once mastered, may be successfully used to accurately measure dissolved carbon monoxide concentrations. [Pg.44]

An instrument that combines the advantages of MALDI ionization, TOP mass analyzer, and aerosol sampling was developed by van Wuijckhuijse and coworkers in The Netherlands [31]. Standard samples were prepared by mixing insulin, cytochrome-c, or myoglobin in dis-... [Pg.429]


See other pages where Myoglobin sample preparation is mentioned: [Pg.907]    [Pg.916]    [Pg.139]    [Pg.721]    [Pg.47]    [Pg.626]    [Pg.525]    [Pg.164]    [Pg.147]    [Pg.127]    [Pg.288]    [Pg.239]    [Pg.177]    [Pg.229]    [Pg.52]    [Pg.114]    [Pg.185]    [Pg.44]    [Pg.45]    [Pg.105]    [Pg.149]    [Pg.345]   
See also in sourсe #XX -- [ Pg.871 ]




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