作者: Johan Sjödahl , Åsa Emmer , Jan Vincent , Johan Roeraade
DOI: 10.1016/S1046-5928(02)00519-3
关键词: Carboxypeptidase A 、 Protease 、 Carboxypeptidase activity 、 Enzyme 、 Capillary electrophoresis 、 Chromatography 、 Biochemistry 、 Chemistry 、 Euphausia 、 Substrate (chemistry) 、 Mass spectrometry
摘要: Abstract Fractions of three trypsin-like proteinases, TL I, II, and III, a chymotrypsin-like proteinase, CL, two carboxypeptidase A enzymes, CPA I II B CPB from Antarctic krill ( Euphausia superba ) have been characterized with respect to purity by the means capillary electrophoresis, CE, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS). The masses proteinases were determined be 25,020, 25,070, 25,060, 26,260 Da for respectively. enzymes are likely 23,170 23,260 Da, whereas enzyme 33,730 33,900 Da. degradation efficiency cleavage pattern studied native myoglobin as model substrate using MALDI-TOF-MS, nanoelectrospray (nESI-MS). was found approximately 12 60 times higher compared bovine trypsin at 37 °C 1–3 °C, All fractions showed activity in combination their activity.