Characteristics of a glucose matrix in 252 Cf-plasma desorption mass spectrometry /
The use of glucose film as matrix for 252CF-plasma
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| Format: | Thesis Book |
| Language: | English |
| Published: |
[Place of publication not identified] :
[publisher not identified] ;
1995.
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| Subjects: | |
| Online Access: | Link to OAKTrust copy http://proxy.library.tamu.edu/login?url=http://proquest.umi.com/pqdweb?did=742745601&sid=1&Fmt=2&clientId=2945&RQT=309&VName=PQD |
| Summary: | The use of glucose film as matrix for 252CF-plasma desorption mass spectrometry (PDMS) analysis was explored in this study. To characterize this glucose matrix, simple salts, hydrophobic salts, and biomolecules were analyzed. The results of simple salts indicate that sufficient salvation of the ions by glucose matrix can only be realized at mole fractions no more than 0.01. The hydrophobic ions were found to concentrate on the glucose film surface, similar to their behavior in the solution phase. In the analysis of amino acids, pH study was carried out. The ion yields are not totally correlated with the ion concentration in the solution phase, suggesting the effect of gas phase reaction. For peptide samples, surface effect was observed in concentration study and mixture study, another indication that the glucose film mimics the solution phase. Fragmentation of the peptides in glucose films was also investigated. Positive fragment ions were detected for the tripeptides while positive and negative fragment ions were observed for angiotensin 11 and reduce bovine insulin A- chain. The negative fragmentation of peptides in PDMS has not been observed or discussed before. Both positive and negative fragmentation patterns suggest the charge-remote fragmentation mechanism. The interaction of biomolecules and CU(II) ions was investigated in glucose films. The CU(II) complex ions with amino acids and peptides were detected. I- Es residue shows strong CU(II) binding ability. The biomolecule samples were analyzed by capillary electrophoresis (CE), which shows electrophoretic mobility changes after CU(II) ion binding. The charge state for the CU(IT) complex suggests that protons in the blomolecules are replaced when binding the CU(II) ions. |
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| Item Description: | Vita. "Major Subject: Chemistry". In title, numerals and subscripts are used. |
| Physical Description: | xiv, 175 leaves : illustrations ; 28 cm. Issued also on microfiche from University Microfilms Inc. |
| Bibliography: | Includes bibliographical references. |