Primary structure of rat lysozyme.
For evolutionary reasons, we determined the primary structure of rat lysozyme. The chymotryptic peptides from the reduced and carboxymethylated protein were sequenced and aligned by homology with the sequence of human lysozyme. Overlaps were confirmed by partial structures of tryptic peptides and an automatic sequencer run on the whole protein. By comparing this lysozyme sequence with those of human and baboon and taking into account paleontological estimates of the times of divergence of these species from one another, an approximate estimate of the average rate of lysozyme evolution was made. This rate is not significantly different from the average rate of lactalbumin evolution in mammals--a finding which is at variance with Dickerson's [Dickerson, R.E. (1971), J. Mol. Evol. 1, 26] and Dayhoff's [Dayhoff, m.o., ed. (1972), Atlas of Protein Structure and Sequence, Vol. 5, Silver Spring, Md., The National Biomedical Research Foundation] conclusion that lactalbumin evolution has been faster than lysozyme evolution. Our finding raises the possibility that the gene duplication event responsible for the origin of lactalbumin from lysozyme was more ancient than is generally supposed. Furthermore, from comparison of the rates of lysozyme evolution in rodents and primates, it is suggested that generation time is not a key factor in lysozyme evolution.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D005075:Biological Evolution; D002918:Chymotrypsin; D009113:Muramidase / Q000652:urine; D010446:Peptide Fragments / Q000032:analysis; D051381:Rats; D013045:Species Specificity
D000596:Amino Acids; D010446:Peptide Fragments; D009113:Muramidase; D002918:Chymotrypsin