Methods for alkaline hydrolysis of proteins and chromatographic resolution and quantitation of the calcium-binding amino acid y-carboxyglutamate (Gla) are presented. Gla is extremely acid labile and totally converted to glutamic acid during acid hydrolysis. Under the recommended hydrolysis condition
Chemotactic activity of theγ-carboxyglutamic acid containing protein in bone
✍ Scribed by Gregory R. Mundy; James W. Poser
- Publisher
- Springer
- Year
- 1983
- Tongue
- English
- Weight
- 393 KB
- Volume
- 35
- Category
- Article
- ISSN
- 1432-0827
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We report the first direct method for the identification of the vitamin K-dependent Ca2+ binding amino acid, gamma-carboxyglutamic acid (Gla), in the sequencing of proteins. The carboxyl groups on the protein are first converted to methyl esters with methanolic HCl, a procedure that reduces the pola
A method for the chemical modification of y-carboxyglutamic acid (Gla) residues in proteins is introduced that has the combined advantages of mildness, a high degree of specificity, and the ability to introduce a radiolabel at modification sites for ease in quantitation. Unlike other Gla modificatio