Amino-acid sequence of an alpha-parvalbumin, pI = 4.88, from frog skeletal muscle.
The primary structure of the most basic (pI = 4.88) of the two major parvalbumins from frog skeletal muscle (Rana esculenta) has been determined by partial automatic sequencing of the protein which exhibits a free N terminus, and a study of overlapping peptides obtained by cyanogen bromide cleavage and digestion with trypsin, thermolysin and Armillaria mellea protease. This protein shows the typical structure of an alpha-parvalbumin. Comparison of the primary structure of ion-binding loops of alpha and beta-parvalbumins does not provide a clear-cut explanation of their differences in ion-binding properties.
D000363:Agaricales / Q000201:enzymology; D000595:Amino Acid Sequence; D000818:Animals; D003488:Cyanogen Bromide; D007526:Isoelectric Point; D009124:Muscle Proteins; D009132:Muscles / Q000032:analysis*; D010320:Parvalbumins; D010446:Peptide Fragments; D010447:Peptide Hydrolases; D011893:Rana esculenta; D013820:Thermolysin; D014357:Trypsin
D009124:Muscle Proteins; D010320:Parvalbumins; D010446:Peptide Fragments; D010447:Peptide Hydrolases; D014357:Trypsin; D013820:Thermolysin; D003488:Cyanogen Bromide