Studies on the structure of aldolase A from chicken muscle.
S-Carboxymethylated chicken muscle aldolase was treated with cyanogen bromide to cleave the 4 methionyl bonds per subunit. Five homogeneous fractions were obtained designated fragments I-V. Fragment I was derived from the N-terminus and fragment II from the C-terminus of the enzyme. Reduction of the enzyme with NaB3H4 in the presence of dihydroxyacetone phosphate decreases the enzymatic activity by 90%. Fragment III contained the Schiff base-forming lysine residue since more than 83% of the radioactivity introduced by NaB3H4 reduction of aldolase-dihydroxyacetone phosphate was found in this fraction. A tryptic peptide of 27 amino acid residues containing the substrate-binding site was isolated. The gross molecular structure of aldolase A from chicken muscle indicates a high degree of homology with mammalian muscle aldolases.
D000478:Alkylation; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D002645:Chickens / Q000378:metabolism*; D003488:Cyanogen Bromide; D005634:Fructose-Bisphosphate Aldolase; D009132:Muscles / Q000201:enzymology*; D010446:Peptide Fragments / Q000302:isolation & purification; D013045:Species Specificity; D014357:Trypsin
D000596:Amino Acids; D010446:Peptide Fragments; D014357:Trypsin; D005634:Fructose-Bisphosphate Aldolase; D003488:Cyanogen Bromide