HEWL, although it has 16 substitutions and
1 deletion in the 48 N-terminal amino acids. Distant relationships with HEWL are also discernible in the lysozymes of the frog Rana pipiens, the
trout Onkorhynchus mykiss and the plaice Pleuronectes platessa [64]. Although it is generally
agreed that a-lactalbumin originated from a lysozyme, there is some disagreement as to when this
occurred. According to one model of evolution,
the gene duplication between lysozyme and alactalbumin occurred before, or shortly after, the
separation of the mammals and the birds. This
model avoids the assumption of accelerated
evolution of the a-lactalbumin line, and explains
why a-lactalbumin and the mammalian lysozymes
resemble the c-type lysozymes of the birds and
reptiles to a similar degree. According to an
alternative model, the a-lactalbumin gene arose
at the beginning of mammalian evolution, at the
same time as the appearance of the milk gland.
This model assumes a higher rate of evolution for
a-Iactalbumins than for lysozymes [197, 216].
Because of a shortage of sequence data, little
can be said definitively either about the evolutionary relationships between the lysozymes of
vertebrates and invertebrates, or about the total
number of lysozyme types to be found in the animal kingdom. The lysozyme of the moth Hyalophora cecropia agrees in about 40 % of its 120
amino acids with HEWL. The lysozymes of the
moths Bombyx mori, Galleria melonella and Spodoptera littoralis are significantly homologous in
the 33 N-terminal amino acids to HEWL and
human lysozyme, and have about the same size of
15-16 kDa [260]. Results obtained with the
enzyme-linked immunosorbent assay (ELISA)
method, which allows the detection of distant
immunological relationships, suggest that the
lysozymes of the migratory locust Locusta migratoria and various avian c types are quite similar,
although the sequence similarities show only
about 60 % agreement [116]. In contrast, the lysozyme of the Mediterranean fruit fly Ceratitis capitata with a mass of 23 kDa (210 amino acids) is
much larger than the other known lysozymes, and
with its chitinase activity shows different enzymatic properties. The lysozyme of the starfish
Asterias rubens differs consistently from all other
lysozymes in its length of 142 amino acids, Nterminal sequence and functional properties. On
the other hand, the lysozyme of the polychaete
Nephthys hombergi is similar to type-c vertebrate
enzymes, at least in its enzymatic activity; however, in this case, there are as yet no sequence
data.
References
505
References
1. Agnisola C., Salvadore S. and Scardi Y.: On the occurrence of cellulolytic activity in the digestive gland of
some marine carnivorous molluscs. Compo Biochem.
Physiol. Pt. B 70: 521-525 (1981)
2. Allen A.: Mucus - A protective secretion of complexity. Trends biochem. Sci. 8: 169-173 (1983)
3. Altman P. L. and Dittmer D. S. (eds.): Biological data
book, 2. ed., Vol. III, pp. 1936-42. Fed. Amer. Soc.
Exp. BioI., Bethesda 1974
4. Andersen S. 0.: Sclerotization and tanning of the
cuticle. In: Kerkut G. A. and Gilbert L. I. (eds.):
Comprehensive insect physiology, biochemistry and
pharmacology, Vol. 3, pp. 59-75. Pergamon Press,
Oxford 1985
5. Antonsson P., Heinegard D. and Oldberg A.:
The keratan sulfate-enriched region of bovine cartilage
proteoglycan consists of a consecutively repeated hexapeptide motif. J. BioI. Chern. 264: 16170-73 (1989)
6. Aon M. A. and Curtino J. A.: Protein-bound glycogen
is linked to tyrosine residues. Biochem. J. 229:
269-272 (1985)
7. Arslan A., Standifer L. N. and Don H.: Carbohydrates in honey bee hemolymph. Compo Biochem. Physiol. Pt B 84: 363-367 (1986)
8. Atkins E. D. T., Dlugosz J. and Foord S.: Electron diffraction and electron microscopy of crystalline a-chitin
from the grasping spines of the marine worm Sagitta.
Int. J. bioI. Macromol. 1: 29 (1979)
9. Bai G. et al.: The primary structure of rat liver glycogen synthase deduced by cDNA cloning. Absence of
phosphorylation sites la and lb. J. BioI. Chern. 265:
7843-48 (1990)
10. Bailey C. J., Geoffroy P. and Mills K. H. G.: An examination of the distribution of hen- and goose-type
lysozymes in Anseriformes. Compo Biochem. Physiol.
Pt. B 55: 429-433 (1976)
11. Baker J. E.: Properties of amylases from midguts of
larvae of Sitophilus zeamais and Sitophilus granarius.
Insect Biochem. 13: 421-428 (1983)
12. Baker M. E.: A common ancestor for human placental
17B-hydroxysteroid dehydrogenase, Streptomyces
coelicolor act III protein, and Drosophila melanogaster alcohol dehydrogenase. Faseb J. 4: 222-226
(1990)
13. Bakken H.: Cold hardiness in the alpine beetles Patrobus septentrionis and Cathus melanocephalus. J.
Insect Physiol. 31: 447-453 (1985)
14. Ballas R. A., Garavelli J. S. and White III H. B.:
Estimation of the rate of glycerol-3-phosphate dehydrogenase evolution in higher vertebrates. Evolution
38: 658-664 (1984)
15. Bangs J. D. et aI.: Biosynthesis of a variant surface
glycoprotein of Trypanosoma brucei. Processing of the
glycolipid anchor and N-linked oligosaccharides. J.
BioI. Chern. 263: 17697-705 (1988)
16. Barboza P. S. and Hume I. D.: Hindgut fermentation
in the wombats: two marsupial grazers. J. compo PhysioI. B 162: 561-566 (1992)
17. Barretto O. C. O. et aI.: Erythrocyte sorbitol dehydrogenase of selected nonmammalian species. Compo
Biochem. PhysioI. Pt. B 82: 317-319 (1985)
18. Batterham P. et aI.: Origin and expression of an alcohol dehydrogenase gene duplication in the genus Drosophila. Evolution 38: 644-657 (1984)
1 deletion in the 48 N-terminal amino acids. Distant relationships with HEWL are also discernible in the lysozymes of the frog Rana pipiens, the
trout Onkorhynchus mykiss and the plaice Pleuronectes platessa [64]. Although it is generally
agreed that a-lactalbumin originated from a lysozyme, there is some disagreement as to when this
occurred. According to one model of evolution,
the gene duplication between lysozyme and alactalbumin occurred before, or shortly after, the
separation of the mammals and the birds. This
model avoids the assumption of accelerated
evolution of the a-lactalbumin line, and explains
why a-lactalbumin and the mammalian lysozymes
resemble the c-type lysozymes of the birds and
reptiles to a similar degree. According to an
alternative model, the a-lactalbumin gene arose
at the beginning of mammalian evolution, at the
same time as the appearance of the milk gland.
This model assumes a higher rate of evolution for
a-Iactalbumins than for lysozymes [197, 216].
Because of a shortage of sequence data, little
can be said definitively either about the evolutionary relationships between the lysozymes of
vertebrates and invertebrates, or about the total
number of lysozyme types to be found in the animal kingdom. The lysozyme of the moth Hyalophora cecropia agrees in about 40 % of its 120
amino acids with HEWL. The lysozymes of the
moths Bombyx mori, Galleria melonella and Spodoptera littoralis are significantly homologous in
the 33 N-terminal amino acids to HEWL and
human lysozyme, and have about the same size of
15-16 kDa [260]. Results obtained with the
enzyme-linked immunosorbent assay (ELISA)
method, which allows the detection of distant
immunological relationships, suggest that the
lysozymes of the migratory locust Locusta migratoria and various avian c types are quite similar,
although the sequence similarities show only
about 60 % agreement [116]. In contrast, the lysozyme of the Mediterranean fruit fly Ceratitis capitata with a mass of 23 kDa (210 amino acids) is
much larger than the other known lysozymes, and
with its chitinase activity shows different enzymatic properties. The lysozyme of the starfish
Asterias rubens differs consistently from all other
lysozymes in its length of 142 amino acids, Nterminal sequence and functional properties. On
the other hand, the lysozyme of the polychaete
Nephthys hombergi is similar to type-c vertebrate
enzymes, at least in its enzymatic activity; however, in this case, there are as yet no sequence
data.
References
505
References
1. Agnisola C., Salvadore S. and Scardi Y.: On the occurrence of cellulolytic activity in the digestive gland of
some marine carnivorous molluscs. Compo Biochem.
Physiol. Pt. B 70: 521-525 (1981)
2. Allen A.: Mucus - A protective secretion of complexity. Trends biochem. Sci. 8: 169-173 (1983)
3. Altman P. L. and Dittmer D. S. (eds.): Biological data
book, 2. ed., Vol. III, pp. 1936-42. Fed. Amer. Soc.
Exp. BioI., Bethesda 1974
4. Andersen S. 0.: Sclerotization and tanning of the
cuticle. In: Kerkut G. A. and Gilbert L. I. (eds.):
Comprehensive insect physiology, biochemistry and
pharmacology, Vol. 3, pp. 59-75. Pergamon Press,
Oxford 1985
5. Antonsson P., Heinegard D. and Oldberg A.:
The keratan sulfate-enriched region of bovine cartilage
proteoglycan consists of a consecutively repeated hexapeptide motif. J. BioI. Chern. 264: 16170-73 (1989)
6. Aon M. A. and Curtino J. A.: Protein-bound glycogen
is linked to tyrosine residues. Biochem. J. 229:
269-272 (1985)
7. Arslan A., Standifer L. N. and Don H.: Carbohydrates in honey bee hemolymph. Compo Biochem. Physiol. Pt B 84: 363-367 (1986)
8. Atkins E. D. T., Dlugosz J. and Foord S.: Electron diffraction and electron microscopy of crystalline a-chitin
from the grasping spines of the marine worm Sagitta.
Int. J. bioI. Macromol. 1: 29 (1979)
9. Bai G. et al.: The primary structure of rat liver glycogen synthase deduced by cDNA cloning. Absence of
phosphorylation sites la and lb. J. BioI. Chern. 265:
7843-48 (1990)
10. Bailey C. J., Geoffroy P. and Mills K. H. G.: An examination of the distribution of hen- and goose-type
lysozymes in Anseriformes. Compo Biochem. Physiol.
Pt. B 55: 429-433 (1976)
11. Baker J. E.: Properties of amylases from midguts of
larvae of Sitophilus zeamais and Sitophilus granarius.
Insect Biochem. 13: 421-428 (1983)
12. Baker M. E.: A common ancestor for human placental
17B-hydroxysteroid dehydrogenase, Streptomyces
coelicolor act III protein, and Drosophila melanogaster alcohol dehydrogenase. Faseb J. 4: 222-226
(1990)
13. Bakken H.: Cold hardiness in the alpine beetles Patrobus septentrionis and Cathus melanocephalus. J.
Insect Physiol. 31: 447-453 (1985)
14. Ballas R. A., Garavelli J. S. and White III H. B.:
Estimation of the rate of glycerol-3-phosphate dehydrogenase evolution in higher vertebrates. Evolution
38: 658-664 (1984)
15. Bangs J. D. et aI.: Biosynthesis of a variant surface
glycoprotein of Trypanosoma brucei. Processing of the
glycolipid anchor and N-linked oligosaccharides. J.
BioI. Chern. 263: 17697-705 (1988)
16. Barboza P. S. and Hume I. D.: Hindgut fermentation
in the wombats: two marsupial grazers. J. compo PhysioI. B 162: 561-566 (1992)
17. Barretto O. C. O. et aI.: Erythrocyte sorbitol dehydrogenase of selected nonmammalian species. Compo
Biochem. PhysioI. Pt. B 82: 317-319 (1985)
18. Batterham P. et aI.: Origin and expression of an alcohol dehydrogenase gene duplication in the genus Drosophila. Evolution 38: 644-657 (1984)