NMR studies on parvalbumin phylogeny and ionic interactions.
The inspection of several muscular parvalbumins from different species by two NMR methods (113Cd resonance and 1H relaxation measurements) allows two classes of parvalbumins to be distinguished according to their ion-binding properties. This result is in agreement with the phylogenetic classification of parvalbumins in two series, alpha and beta, which was established on the basis of the primary structures of these proteins. All parvalbumins are characterized by the presence of two primary cationic sites CD and EF, with structural features closely related to those already known on the basis of X-ray crystallographic studies of the beta parvalbumin pI 4.25 from carp muscle. However, parvalbumins of the beta series are characterized by a secondary cation (Ca2+, Mg2+ and other cations) binding site which is absent (or at least inaccessible) in parvalbumins of the alpha series. The major component from thornback ray (pI 4.45) behaves as an alpha parvalbumin as shown by the present NMR studies, although its primary structure suggests a closer similarity with the parvalbumins of the beta series.
D000818:Animals; D002104:Cadmium; D005399:Fishes; D007554:Isotopes; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D008345:Manganese / Q000378:metabolism; D009124:Muscle Proteins / Q000032:analysis*; D010320:Parvalbumins / Q000032:analysis* / Q000235:genetics; D010802:Phylogeny; D011817:Rabbits
D007554:Isotopes; D009124:Muscle Proteins; D010320:Parvalbumins; D002104:Cadmium; D008345:Manganese