Primary structure of parvalbumin from rat skeletal muscle.
The primary structure of parvalbumin from rat skeletal muscle has been determined principally by automated sequencing of tryptic peptides using 4-N,N-dimethylaminoazobenzene 4'-isothiocyanate as the Edman reagent on a solid-phase sequencer. Remaining positions and most peptide overlaps were identified by analysis of peptides arising from CNBr, chymotryptic and Staphylococcus aureus protease cleavages and through digestions with carboxypeptidases A, B and Y. Reverse-phase high-performance liquid chromatography on C-18 supports was employed for all peptide separations. Structural homology between rat and rabbit parvalbumins helped to confirm the alignments of the tryptic peptides T4-T3, T2-T6 and to define the position of the Lys triplet (36-38). A comparison of the two mammalian proteins revealed 14 amino acid differences, which are all located on the surface of the molecule. A prediction of the secondary structure has been made and found to be very similar for the rat and rabbit proteins with the exception of the sequence region 72-78, located between the Ca2+, Mg2+-binding CD and EF domains.
D000595:Amino Acid Sequence; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D002918:Chymotrypsin; D003488:Cyanogen Bromide; D009124:Muscle Proteins / Q000302:isolation & purification*; D009132:Muscles / Q000032:analysis*; D010320:Parvalbumins / Q000302:isolation & purification*; D010446:Peptide Fragments / Q000302:isolation & purification; D010447:Peptide Hydrolases; D051381:Rats
D009124:Muscle Proteins; D010320:Parvalbumins; D010446:Peptide Fragments; D010447:Peptide Hydrolases; D002918:Chymotrypsin; D003488:Cyanogen Bromide