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. 1985 Aug;4(8):2119–2122. doi: 10.1002/j.1460-2075.1985.tb03901.x

Amino acid and cDNA sequences of lysozyme from Hyalophora cecropia

Å Engström 1, K G Xanthopoulos 1, H G Boman 1, H Bennich 1
PMCID: PMC554471  PMID: 16453632

Abstract

The amino acid and cDNA sequences of lysozyme from the giant silk moth Hyalophora cecropia have been determined. This enzyme is one of several immune proteins produced by the diapausing pupae after injection of bacteria. Cecropia lysozyme is composed of 120 amino acids, has a mol. wt. of 13.8 kd and shows great similarity with vertebrate lysozymes of the chicken type. The amino acid residues responsible for the catalytic activity and for the binding of substrate are essentially conserved. Three allelic variants of the Cecropia enzyme are identified. A comparison of the chicken and the Cecropia lysozymes shows that there is a 40% identity at both the amino acid and the nucleotide level. Some evolutionary aspects of the sequence data are discussed.

Keywords: invertebrate lysozyme, amino acid sequence, cDNA sequence, insect immunity, protein evolution

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Selected References

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