J. Biochem, 1995, Vol. 118, No. 3 546-551
© 1995 Japanese Biochemical Society
other |
Insect Lysozyme from House Fly (Musca domestica) Larvae: Possible Digestive Function Based on Sequence and Enzymatic Properties
Graduate School of Pharmaceutical Sciences, Kyushu University Maidashi, Higashi-ku, Fukuoka 812-82
1To whom correspondence should be addressed. email: imoto{at}imml.phar.kyushu-u.ac.jp
Lysozyme was purified from the homogenate of the whole body of house fly (Musca domestica) larvae by standard chromatographic techniques. The purified lysozyme was sequenced and its enzymatic properties were examined. This lysozyme was a chicken–type lysozyme composed of 122 amino acids, showing about 75% identity with fruit fly lysozymes and 38% with human lysozyme. This enzyme was inactive towards Micrococcus luteus under the physiological conditions of pH 7.0 and ionic strength 0.1, but was as active towards glycol chitin as was hen lysozyme. The pH–dependent profile of lytic activity towards M. luteus showed that house fly lysozyme has an acidic pH optimum and shows no enzymatic activity above pH 7. These features are analogous with those of ruminant stomach lysozymes which have evolved for the digestive function, suggesting that this lysozyme does not function as a self-defense protein, like hen and human lysozyme, but as a digestive enzyme, probably in the gut of the insect body. Although a similar functional conversion to digestive enzyme was reported in fruit fly, phylogenetic tree analysis indicates that the evolutionary change of lysozyme to a digestive enzyme occurred similarly in fruit fly and house fly, but the events are not related and occurred independently in each strain. This observation is in contrast with the case of ruminant stomach lysozymes, which were recruited before the divergence of each species of ruminants.