Purification and characterization of pancreatic elastase from Atlantic cod (Gadus morhua).
1. A pancreatic elastase from Atlantic cod (Gadus morhua) has been purified and characterized. 2. The enzyme is a very basic protein with an approximate mol. wt of 28,000. 3. The cod elastase has higher elastin specificity than porcine elastase, and it is inhibited by soybean trypsin inhibitor, which has no effect on porcine elastase. 4. The cod elastase expresses a higher turnover number (kcat) and catalytic efficiency (kcat/Km) than porcine elastase, but it is less thermostable.
Gildberg
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Institute of Fisheries Technology Research, Tromsø, Norway.
Overbø
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D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004549:Elastin / Q000378:metabolism; D005399:Fishes; D007700:Kinetics; D008970:Molecular Weight; D010179:Pancreas / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D013379:Substrate Specificity; D013552:Swine; D014361:Trypsin Inhibitors / Q000494:pharmacology
D000596:Amino Acids; D002241:Carbohydrates; D014361:Trypsin Inhibitors; D004549:Elastin; D010196:Pancreatic Elastase