Parvalbumins from frog skeletal muscle (Rana temporaria L.). Isolation and characterization. Structural modifications associated with calcium binding.
Two parvalbumins have been isolated from the skeletal muscle of Rana temporaria L. Amino acid composition, tryptic peptide maps, isoelectric points, calcium content and ultraviolet as well as circular dichroism spectra have been determined. Investigation on antigenic properties revealed no antigenic determinants common to both components. The two protein molecules appear to belong to far related gene lineages. They are also different from the parvalbumins found in Rana esculenta muscle. Modifications of physical parameters, associated with calcium binding and dissociation are described. While antigenicity remained essentially unchanged, conformational changes were revealed by alterations of circular dichroism spectra.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001001:Anura; D002118:Calcium / Q000032:analysis*; D002942:Circular Dichroism; D005779:Immunodiffusion; D009124:Muscle Proteins / Q000302:isolation & purification; D009132:Muscles / Q000032:analysis*; D010320:Parvalbumins / Q000276:immunology / Q000302:isolation & purification; D011485:Protein Binding; D011489:Protein Denaturation; D011896:Rana temporaria; D013056:Spectrophotometry, Ultraviolet; D013438:Sulfhydryl Compounds / Q000032:analysis
D000596:Amino Acids; D009124:Muscle Proteins; D010320:Parvalbumins; D013438:Sulfhydryl Compounds; D002118:Calcium