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Heat-stable protease from the marine sponge Geodia cydonium.
Cell Mol Biol (Noisy-le-grand). 2002 Jun; 48(4):379-83.CM

Abstract

A protease from the marine sponge Geodia cydonium was purified from an aqueous extract by gel filtration and anion-exchange chromatography. A 200-kDa proteolytically active band was obtained when the enzyme was analyzed in gelatin-copolymerized zymograms. The enzyme was also able to degrade casein, bovine collagen, and the synthetic substrate alpha-N-benzoyl-D-arginine p-nitroanilide (BAPNA). Optimal conditions for proteolytic activity were achieved in the presence of 10 mM CaCl2 and within the pH range 7.0 to 8.5. The protease showed an extraordinary heat resistance. The enzyme activity was inhibited by phenylmethylsulphonyl fluoride (PMSF) and N-tosyl-lysine chloromethyl ketone (TLCK), suggesting that the enzyme belongs to the group of serine-type proteases. We propose that the protease is involved in sponge collagen catabolism.

Authors+Show Affiliations

Wilkesman J
Departamento de Química, Facultad de Ciencias y Tecnología, Universidad de Carabobo, Valencia, Venezuela.
Schröder HC
No affiliation info available

MeSH

AnimalsChromatography, Ion ExchangeEndopeptidasesEnzyme StabilityHot TemperatureHydrogen-Ion ConcentrationKineticsPoriferaSubstrate Specificity

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

12064445

Citation

Wilkesman, Jeff, and Heinz C. Schröder. "Heat-stable Protease From the Marine Sponge Geodia Cydonium." Cellular and Molecular Biology (Noisy-le-Grand, France), vol. 48, no. 4, 2002, pp. 379-83.
Wilkesman J, Schröder HC. Heat-stable protease from the marine sponge Geodia cydonium. Cell Mol Biol (Noisy-le-grand). 2002;48(4):379-83.
Wilkesman, J., & Schröder, H. C. (2002). Heat-stable protease from the marine sponge Geodia cydonium. Cellular and Molecular Biology (Noisy-le-Grand, France), 48(4), 379-83.
Wilkesman J, Schröder HC. Heat-stable Protease From the Marine Sponge Geodia Cydonium. Cell Mol Biol (Noisy-le-grand). 2002;48(4):379-83. PubMed PMID: 12064445.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Heat-stable protease from the marine sponge Geodia cydonium. AU - Wilkesman,Jeff, AU - Schröder,Heinz C, PY - 2002/6/18/pubmed PY - 2003/8/20/medline PY - 2002/6/18/entrez SP - 379 EP - 83 JF - Cellular and molecular biology (Noisy-le-Grand, France) JO - Cell Mol Biol (Noisy-le-grand) VL - 48 IS - 4 N2 - A protease from the marine sponge Geodia cydonium was purified from an aqueous extract by gel filtration and anion-exchange chromatography. A 200-kDa proteolytically active band was obtained when the enzyme was analyzed in gelatin-copolymerized zymograms. The enzyme was also able to degrade casein, bovine collagen, and the synthetic substrate alpha-N-benzoyl-D-arginine p-nitroanilide (BAPNA). Optimal conditions for proteolytic activity were achieved in the presence of 10 mM CaCl2 and within the pH range 7.0 to 8.5. The protease showed an extraordinary heat resistance. The enzyme activity was inhibited by phenylmethylsulphonyl fluoride (PMSF) and N-tosyl-lysine chloromethyl ketone (TLCK), suggesting that the enzyme belongs to the group of serine-type proteases. We propose that the protease is involved in sponge collagen catabolism. SN - 0145-5680 UR - https://www.unboundmedicine.com/medline/citation/12064445/Heat_stable_protease_from_the_marine_sponge_Geodia_cydonium_ DB - PRIME DP - Unbound Medicine ER -