Biomaterial Database

Purification and characterization of two pancreatic elastase isoforms from dogfish (Scyliorhinus canicula). 1995

A Smine, and Y Le Gal

Laboratoire de Biologie Marine du Collège de France, Concarneau.

Two elastase isoforms were isolated from activated pancreatic extract of dogfish (Scyliorhinus canicula). The purification procedures for both elastases included ammonium sulfate fractionation, ion exchange on DEAE cellulose and Mono-QHR column followed by gel filtration on PL-GFS (HPLC) column. The two isoenzymes, EI and EII, exhibit a high activity toward the specific elastase substrate succinyl-(ala)3-p-nitroanilide (SANA) with different kinetic parameters at 37 degrees C. However, the two different enzymes have similar properties on the basis of pH, temperature, and molecular weight study. The activity of both variants was completely inhibited by elastatinal, phenylmethyl sulfonyl fluoride, (PMSF), diisopropyl fluorophosphate, (iPr2-FP), but less by p-chloromercuribenzoic acid (PCMB) and soybean trypsin inhibitor. EI and EII have similar amino acid composition; their amino-terminal sequences have 85% homology with human and rat elastase 2.

UI	MeSH Term	Description	Entries
D007527	Isoenzymes	Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.	Alloenzyme,Allozyme,Isoenzyme,Isozyme,Isozymes,Alloenzymes,Allozymes
D008969	Molecular Sequence Data	Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.	Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010078	Oxazines	Six-membered heterocycles containing an oxygen and a nitrogen.
D010196	Pancreatic Elastase	A protease of broad specificity, obtained from dried pancreas. Molecular weight is approximately 25,000. The enzyme breaks down elastin, the specific protein of elastic fibers, and digests other proteins such as fibrin, hemoglobin, and albumin. EC 3.4.21.36.	Elastase,Pancreatopeptidase,Elastase I,Pancreatic Elastase I,Elastase I, Pancreatic,Elastase, Pancreatic
D002412	Cations	Positively charged atoms, radicals or groups of atoms which travel to the cathode or negative pole during electrolysis.	Cation
D002614	Chelating Agents	Chemicals that bind to and remove ions from solutions. Many chelating agents function through the formation of COORDINATION COMPLEXES with METALS.	Chelating Agent,Chelator,Complexons,Metal Antagonists,Chelators,Metal Chelating Agents,Agent, Chelating,Agents, Chelating,Agents, Metal Chelating,Antagonists, Metal,Chelating Agents, Metal
D004284	Dogfish	Sharks of the family Squalidae, also called dogfish sharks. They comprise at least eight genera and 44 species. Their LIVER is valued for its oil and its flesh is often made into fertilizer.	Squalidae,Dogfishes
D004549	Elastin		alpha-Elastin,kappa-Elastin,alpha Elastin,kappa Elastin
D004791	Enzyme Inhibitors	Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.	Enzyme Inhibitor,Inhibitor, Enzyme,Inhibitors, Enzyme
D004795	Enzyme Stability	The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.	Enzyme Stabilities,Stabilities, Enzyme,Stability, Enzyme