Characterization of proteinases from Antarctic krill (Euphausia superba)

Sjodahl, J. (författare)

Vincent, J. (författare)

(creator_code:org_t)

2002
2002
Engelska.
Ingår i: Protein Expression and Purification. - 1046-5928 .- 1096-0279. ; 26:1, s. 153-161

Relaterad länk:: https://urn.kb.se/re...; visa fler...; https://doi.org/10.1...; visa färre...

Abstract Ämnesord

Stäng

Fractions of three trypsin-like proteinases, TL I, TL II, and TL III, a chymotrypsin-like proteinase, CL, two carboxypeptidase A enzymes, CPA I and CPA II and two carboxypeptidase B enzymes. CPB I and CPB II, from Antarctic krill (Euphausia superba) have been characterized with respect to purity by the means of capillary electrophoresis, CE, and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS). The masses of the trypsin-like and chymotrypsin-like proteinases were determined to be 25,020, 25,070, 25,060. and 26,260 Da for TL I, TL II, TL III, and CL, respectively. The masses of the CPA enzymes are likely 23,170 and 23,260 Da. whereas the CPB enzyme masses likely are 33,730 and 33,900 Da, The degradation efficiency and cleavage pattern of the trypsin-like proteinases were studied with native myoglobin as a model substrate using CE, MALDI-TOF-MS, and nanoelectrospray mass spectrometry (nESI-MS). The degradation efficiency of the trypsin-like proteinases was found to be approximately 12 and 60 times higher compared to bovine trypsin at 37 degreesC and 1-3 degreesC, respectively. All three fractions of trypsin-like proteinases showed a carboxypeptidase activity in combination with their trypsin activity.

Av författaren/redakt...: Sjodahl, J.; Emmer, Åsa; Vincent, J.; Roeraade, Johan

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