Comparison of /sup 125/I-labeled and /sup 14/C-Labeled peptides of the major outer membrane protein of Chlamydia Trachomatis Strain L2/434 separated by high-performance liquid chromatography
The objective of this study was to determine if in-gel chloramine-T radioiodination adequately labels OM proteins to allow for accurate and precise structural comparison of these molecules. Therefore, intrinsically /sup 14/C-amino acid labeled proteins and /sup 125/I-labeled proteins were cleaved with two endopeptidic reagents and the peptide fragments separated by HPLC. A comparison of retention times of the fragments, as determined by differential radiation counting, thus indicated whether /sup 125/Ilabeling identified of all the peptide peaks seen in the /sup 14/Clabeled proteins. Results demonstrated that radioiodination yields complete and accurate information about the primary structure of outer membrane proteins. In addition, it permits the use of extremely small amounts of protein allowing for method optimization and multiple separations to insure reproducibility.
- Research Organization:
- Department of Microbiology, University of Montana, Missoula, Montana
- OSTI ID:
- 6341766
- Journal Information:
- J. Liquid Chromatogr.; (United States), Vol. 8:6
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
ORGANIC
PHYSICAL AND ANALYTICAL CHEMISTRY
PEPTIDES
COMPARATIVE EVALUATIONS
LABELLING
LIQUID COLUMN CHROMATOGRAPHY
STRUCTURAL CHEMICAL ANALYSIS
CARBON 14 COMPOUNDS
CHLORAMINES
COUNTING TECHNIQUES
INDIUM 125
LABELLED COMPOUNDS
MICROORGANISMS
MOLECULAR STRUCTURE
AMINES
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
CHROMATOGRAPHY
INDIUM ISOTOPES
INTERMEDIATE MASS NUCLEI
ISOTOPES
NUCLEI
ODD-EVEN NUCLEI
ORGANIC CHLORINE COMPOUNDS
ORGANIC COMPOUNDS
ORGANIC HALOGEN COMPOUNDS
PROTEINS
RADIOISOTOPES
SEPARATION PROCESSES
400105* - Separation Procedures