Literature DB >> 318409

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

P Lehky1, E A Stein.   

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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Year:  1979        PMID: 318409     DOI: 10.1016/0305-0491(79)90037-3

Source DB:  PubMed          Journal:  Comp Biochem Physiol B        ISSN: 0305-0491


  2 in total

1.  Molar absorptivity and A1 cm (1%) values for proteins at selected wavelengths of the ultraviolet and visible regions. XXII.

Authors:  D M Kirschenbaum
Journal:  Appl Biochem Biotechnol       Date:  1982-11       Impact factor: 2.926

2.  Electrophoretic comparison of the proteins of some perch (Perca fluviatilis L.) head muscles.

Authors:  B Focant; M F Jacob; F Huriaux
Journal:  J Muscle Res Cell Motil       Date:  1981-09       Impact factor: 2.698

  2 in total

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