Jan 1, 1986

Purification and characterization of a proteinase from Euphausia superba Dana (Antarctic krill)

Acta biochimica Polonica
M TurkiewiczM Zielińska


The thiol-dependent serine proteinase (inhibited by DFP, PMSF, pCMB and iodoacetate) was isolated from the whole krill specimens and from the content of the krill digestive tract. The enzyme was purified to homogeneity using a seven-step procedure. Its specific activity with denatured haemoglobin as a substrate was about 6.0 unit/mg. The molecular weight of the enzyme, as determined by gel exclusion chromatography was 33 000 and by polyacrylamide gel electrophoresis with SDS 31 600 (12.5% gel) and 27 000 (7.5% gel). The enzyme is an acidic glycoprotein (pI below 2.9) containing about 5% of carbohydrate. The pH optimum of the enzyme with haemoglobin was 6.0 at the optimal temperature of 40 degrees C in 15-min reaction. The enzyme showed the esterase activity (hydrolysis of BAEE) and was inactive with carbobenzoxy- and benzoyl-dipeptides with the following C-terminal amino acids: Phe, Tyr, Lys, Gly and Leu.

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Mentioned in this Paper

Carboxy-Terminal Amino Acid
Amino Acids, I.V. solution additive
Peptide Hydrolases
Sulfhydryl Compounds
Proteolytic Enzyme
Gel Chromatography
Substrate Specificity

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