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Circular dichroism studies of the Ca2+-binding proteins from the spasmoneme of Carchesium


, : Circular dichroism studies of the Ca2+-binding proteins from the spasmoneme of Carchesium. Comparative Biochemistry and Physiology B Comparative Biochemistry, 814: 927-931

1.1. Ca2+-binding proteins from Carchesium spasmoneme were purified previously, in this study the effects of Ca2+ and Mg2+ on the UV (210–250 nm) circular dichroism of several fractions were studied.2.2. Two fractions showed high affinity for Ca2+ (Km = 2.5 4.5 M), three others did not (Km 20 M).3.3. A purified fraction showed an increase in -helical content with Ca2+, but not with Mg2+.4.4. The -helical content increased with Ca2+ with positive cooperativity (n = 1.6), whereas the cooperativity decreased (n = 1.2) in the presence of Mg2+.5.5. The half-maximal change in -helical content occurred at 4.5 M free Ca2+, which is close to the value obtained in the glycerinated stalk model of Vorticella.

US$19.90

DOI: 10.1016/0305-0491(85)90091-4


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