(4,5-/sup 3/H)lysine:(/sup 14/C)lysine dual-label method to measure lysine hydroxylation in collagen
Journal Article
·
· Anal. Biochem.; (United States)
A new method has been developed to determine the extent of lysine hydroxylation in newly synthesized collagen. This method relies on the measurement of changes in the ratio of (/sup 3/H)lysine:(/sup 14/C)lysine in collagenase digests, resulting from loss of tritium from the C-5 position of lysine during hydroxylation. Lysine hydroxylation can be measured in the presence of large amounts of noncollagen proteins, and simultaneous quantitation of the relative rates of collagen and non-collagen protein production is obtained. The dual-label lysine method is simple, rapid, and accurate. There was a very good correlation between this method and column chromatography procedures currently used for the measurement of lysine hydroxylation.
- Research Organization:
- Veterans Administration Medical Center, San Diego, CA
- OSTI ID:
- 6937284
- Journal Information:
- Anal. Biochem.; (United States), Journal Name: Anal. Biochem.; (United States) Vol. 1; ISSN ANBCA
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AMINO ACIDS
CARBON 14 COMPOUNDS
CARBOXYLIC ACIDS
COLLAGEN
DOUBLE LABELLING
HYDROXYLATION
ISOTOPE APPLICATIONS
ISOTOPE RATIO
LABELLED COMPOUNDS
LABELLING
LYSINE
ORGANIC ACIDS
ORGANIC COMPOUNDS
PROTEINS
SCLEROPROTEINS
TRACER TECHNIQUES
TRITIUM COMPOUNDS
59 BASIC BIOLOGICAL SCIENCES
AMINO ACIDS
CARBON 14 COMPOUNDS
CARBOXYLIC ACIDS
COLLAGEN
DOUBLE LABELLING
HYDROXYLATION
ISOTOPE APPLICATIONS
ISOTOPE RATIO
LABELLED COMPOUNDS
LABELLING
LYSINE
ORGANIC ACIDS
ORGANIC COMPOUNDS
PROTEINS
SCLEROPROTEINS
TRACER TECHNIQUES
TRITIUM COMPOUNDS