Californium-252 plasma desorption mass analysis of proteins adsorbed on polymer and modified-polymer surfaces
A new Cf-252 plasma desorption mass spectrometer has been built specifically for the analysis of large biomolecules. This mass spectrometer was used to investigate the interactions between proteins adsorbed onto polymer surfaces and how the chemical nature of the polymer surface influences the production of stable, gas-phase molecule ions. Chemical modification of the polymer surfaces was achieved by means of ultra-violet irradiation, resulting in the production of a more hydrophilic surface. Analysis of a series of model compounds adsorbed onto modified and non-modified polymer surfaces indicates that the wettability of the surface is an important influence in the production of stable molecular ions. This information was then utilized to aid in the analysis of lysozyme, myoglobin, and porcine trypsin.
- Research Organization:
- Texas A and M Univ., College Station (USA)
- OSTI ID:
- 6107781
- Resource Relation:
- Other Information: Thesis (Ph.D)
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
ORGANIC
PHYSICAL AND ANALYTICAL CHEMISTRY
LYSOZYME
CHEMICAL ANALYSIS
MASS SPECTROSCOPY
PERFORMANCE
MYOGLOBIN
TRYPSIN
CALIFORNIUM 252
DESORPTION
MODIFICATIONS
POLYMERS
SURFACE PROPERTIES
ULTRAVIOLET RADIATION
WETTABILITY
ACTINIDE ISOTOPES
ACTINIDE NUCLEI
ALPHA DECAY RADIOISOTOPES
CALIFORNIUM ISOTOPES
CARBOXYLIC ACIDS
ELECTROMAGNETIC RADIATION
ENZYMES
EVEN-EVEN NUCLEI
GLOBIN
GLYCOSYL HYDROLASES
HEAVY NUCLEI
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
HYDROLASES
ISOTOPES
NUCLEI
O-GLYCOSYL HYDROLASES
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
PEPTIDE HYDROLASES
PIGMENTS
PORPHYRINS
PROTEINS
RADIATIONS
RADIOISOTOPES
SERINE PROTEINASES
SPECTROSCOPY
YEARS LIVING RADIOISOTOPES
400102* - Chemical & Spectral Procedures