APPEARANCE and FATE of A BETA-GALACTANASE, ALPHA,BETA-GALACTOSIDASES, HEPARAN-SULFATE and CHONDROITIN SULFATE DEGRADING ENZYMES DURING DEVELOPMENT of the MOLLUSK POMACEA SP
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Data
1994-08-18
Autores
Oliveira, F. W.
Chavante, S. F.
Santos, E. A.
Dietrich, C. P.
Nader, H. B.
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Artigo
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The characterization and properties of a beta-galactanase and alpha- and beta-galactosidases as well as heparan sulfate and chondroitin sulfate degrading enzymes which appear during the 15 days of the embryonic development of the mollusc Pomacea sp. is reported. the beta-galactanase, which appears around day 7 of development, was separated from alpha- and beta-galactosidase which emerge at day 1 and 4 after oviposition, respectively. the galactanase seems to be responsible for the degradation of an acidic beta-galactan (which is also synthesized by the eggs around day 5) to galactose and di- and tri-galactosides. Heparan sulfate appears around day 10 of development together with a heparan sulfate endoglucuronidase responsible for the degradation of its N-acetylated region. An alpha-N-acetylglucosaminidase and a beta-glucuronidase which act upon the N-acetylated fragments formed from heparan sulfate emerge around day 4 of development. Chondroitin sulfate and a chondroitin sulfate sulfatase emerge around day 9 of development whereas a beta-N-acetylgalactosaminidase and the beta beta-galactan, heparan and chondroitin sulfate, respectively. the possible role of these elements in the migration of mesenchymal cells, in the processes of cell-cell recognition and control of cell growth is discussed.
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Biochimica Et Biophysica Acta-general Subjects. Amsterdam: Elsevier B.V., v. 1200, n. 3, p. 241-248, 1994.