Isolation and characterization of a protease from the marine sponge Spheciospongia vesparia.
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.
Arreguín
R
R
Instituto de Química, Universidad Nacional Autónoma de México, D.F.
Arreguín
B
B
Soriano-García
M
M
Hernández-Arana
A
A
Rodríguez-Romero
A
A
D000818:Animals; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D010450:Endopeptidases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D008970:Molecular Weight; D011161:Porifera / Q000201:enzymology*; D013379:Substrate Specificity
D010450:Endopeptidases