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Isolation and characterization of a protease from the marine sponge Spheciospongia vesparia
Author(s) -
Arreguín R.,
Arreguín B.,
Soriano-García M.,
Hernández-Arana A.,
Rodríguez-Romero A.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80593-j
Subject(s) - sponge , isolation (microbiology) , protease , chemistry , biology , microbiology and biotechnology , biochemistry , enzyme , paleontology
A protein that showed activity against proteic (casein and hide powder azure) and synthetic (BAEE and HLPA) substrates was isolated from the marine sponge Spheciospongia vesparia . The protease was purified from an aqueous extract by ammonium sulfate precipitation, gel filtration, hydrophobic and HPLC‐anion exchange chromatographies. The purified protease showed a single band in SDS‐PAGE minigels and had a molecular weight of 29,600, but when submitted to isoelectric focusing it showed 2 bands with isoelectric points of 4.56 and 4.43. Its catalytic action was inhibited by EDTA and 1,10‐phenanthroline, so it seemed to be a metalloprotease.