The NH2-terminal amino acid sequence of a y-carboxyglutamic acid-containing protein from rat femur cortical bone

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Abstract
The amino acid sequence of 31 NH2-terminal residues of a .gamma.-carboxyglutamic acid (Gla)-containing protein from rat femur cortical bone was determined by the manual Edman degradation method. The phenylthiohydantoin derivative of Gla was directly identified by high performance liquid chromatography. The 31 amino acid sequence was as follows: Tyr-Leu-Asn-Asp-Gly-Leu-Gly-Ala-Hyp-Ala-Pro-Tyr-Pro-Asp-Pro-Leu-Gla-Pro-x-(Arg)-Gla-Val-(Cys)-Gla-Leu-Asn-Pro-Asp-(Cys)-Asp-Glu. The NH2-terminal amino acid sequence over 31 amino acid residues in the rat bone Gla-containing protein was compared to the sequence in those of bovine, human and swordfish proteins. The biological importance of the highly conservative region from the position 20-31, which contained 2 Gla residues and probably a single disulfide bond at the position 23 and 29, and of the as yet undetermined COOH-terminal region is discussed.

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