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.
Arreguín
R
R
Instituto de Química, Universidad Nacional Autónoma de México, Ciudad Universitaria, México.
Arreguín
B
B
Hernández-Arana
A
A
Rodríguez-Romero
A
A
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