Metal content and conformation of the metalloprotease from the marine sponge Spheciospongia vesparia.
We have recently purified a protease from the marine sponge Spheciospongia vesparia. It consists of a single nonglycosylated polypeptide chain with a molecular weight of 29 600 and has one free thiol group. Metal analysis revealed the presence of zinc at 2.02 +/- 0.05 g-atoms per mole of protein, as measured by atomic absorption spectroscopy. The circular dichroism spectrum in the far UV region (183-259 nm) indicates that the sponge protease contains appreciable amounts of beta sheet. This enzyme resembles very much an aminopeptidase from Aeromonas proteolytica concerning activity and some physiochemical characteristics.
Instituto de Química, Universidad Nacional Autónoma de México, Ciudad Universitaria, México.
R
R
Arreguín
B
B
Arreguín
A
A
Hernández-Arana
A
A
Rodríguez-Romero
D000333:Aeromonas / Q000201:enzymology; D000596:Amino Acids / Q000032:analysis; D000626:Aminopeptidases / Q000737:chemistry; D000818:Animals; D002942:Circular Dichroism; D008666:Metalloendopeptidases / Q000737:chemistry* / Q000302:isolation & purification; D008970:Molecular Weight; D011161:Porifera / Q000201:enzymology*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D013054:Spectrophotometry, Atomic; D013056:Spectrophotometry, Ultraviolet; D013438:Sulfhydryl Compounds / Q000032:analysis; D015032:Zinc / Q000032:analysis*
D000596:Amino Acids; D013438:Sulfhydryl Compounds; D000626:Aminopeptidases; D008666:Metalloendopeptidases; D015032:Zinc