Perch muscle parvalbumin: general characterization and magnesium-binding properties.

Comp Biochem Physiol B

Department of Biochemistry, University of Geneva, Switzerland.

Published: July 1989

AI Article Synopsis

  • Parvalbumin exists in two main forms, with concentrations of 2.5 and 3.2 g per kg in fresh muscle.
  • The two forms are 81% similar in amino acid composition but have distinct immune properties.
  • Parvalbumin binds magnesium alongside calcium, and research suggests it may stay in a magnesium-bound state during muscle contraction and relaxation, which is important for understanding its function.

Article Abstract

1. Parvalbumin exists in two major forms, amounting to 2.5 and 3.2 g per kg of fresh muscle. 2. The composition divergence index between both forms, calculated from their amino acid composition, indicates 81% sequence identity; however both isoparvalbumins are immunologically distinct. 3. Beside Ca2+, perch parvalbumin binds 2 g atoms Mg2+ per mol with a dissociation constant of 10(-5) M. 4. Determination of the affinity for magnesium is of particular importance as there are indications that, in vivo, parvalbumin can remain in the Mg2+-state during the contraction-relaxation cycle instead of switching from the Ca2+-to the Mg2+-state and vice versa.

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Source
http://dx.doi.org/10.1016/0305-0491(79)90037-3DOI Listing

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