Close coorelation of atomic absorption measurements for Ca(II) contents indicates that from pH 5.8-7.4 a twentyfold excess of EGTA1 removes but one of two Ca(II) from carp parvalbumin. Thus binding of the two Ca(II) appears to be noncooperative. The maximum in emission intensity observed at a nonint
โฆ LIBER โฆ
Calcium-binding proteins: calcium(II)-lanthanide(III) exchange in carp parvalbumin
โ Scribed by Williams, Thomas C.; Corson, David C.; Sykes, Brian D.
- Book ID
- 115447626
- Publisher
- American Chemical Society
- Year
- 1984
- Tongue
- English
- Weight
- 683 KB
- Volume
- 106
- Category
- Article
- ISSN
- 0002-7863
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To elucidate the physiological role of the Ca2+ binding protein parvalbumin, we have generated transgenic mice carrying the full-length complementary DNA (cDNA) of rat parvalbumin under the control of the heavy-metal inducible metallothionein IIA promoter. Immunohistochemical and biochemical methods