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Calcium affinity of the NH2-terminal epidermal growth factor-like module of factor X. Effect of the gamma-carboxyglutamic acid-containing module.
Valcarce C, Selander-Sunnerhagen M, Tämlitz AM, Drakenberg T, Björk I, Stenflo J. Valcarce C, et al. Among authors: stenflo j. J Biol Chem. 1993 Dec 15;268(35):26673-8. J Biol Chem. 1993. PMID: 8253800 Free article.
In the NMR structure of the NH2-terminal EGF-like module in factor X, five calcium ligating groups have been identified (Selander-Sunnerhagen, M., Ullner, M., Persson, E., Teleman, O., Stenflo, J., and Drakenberg, T. (1992) J. Biol. Chem. 267, 19642-19649). . …
In the NMR structure of the NH2-terminal EGF-like module in factor X, five calcium ligating groups have been identified (Selander-Sunnerhage …
Structural requirements for Ca2+ binding to the gamma-carboxyglutamic acid and epidermal growth factor-like regions of factor IX. Studies using intact domains isolated from controlled proteolytic digests of bovine factor IX.
Astermark J, Björk I, Ohlin AK, Stenflo J. Astermark J, et al. Among authors: stenflo j. J Biol Chem. 1991 Feb 5;266(4):2430-7. J Biol Chem. 1991. PMID: 1989994 Free article.
A comparison with similar studies of factor X (Persson, E., Bjork, I., and Stenflo, J. (1991) J. Biol. Chem. 266, 2444-2452) suggests that the Ca2(+)-induced fluorescence quenching is due to an altered environment primarily around the tryptophan residue in po …
A comparison with similar studies of factor X (Persson, E., Bjork, I., and Stenflo, J. (1991) J. Biol. Chem. 266, 2444- …
159 results