title: [Purification and properties of serine proteinases from European catfish Silurus glanis L. pancreas].
abstract: Three trypsin isoforms (designated as T1, T2, and T3), three chymotrypsin isoforms (Kh1, Kh2, and Kh3), and two elastase isoforms (E1 and E2) were isolated from the pancreas of European catfish Silurus glanis L. by salting out with (NH4)2SO4, gel chromatography on Sephadex G-75, and ion exchange chromatography on DEAE cellulose. Isoelectric points of the enzymes, determined by isoelectric focusing, amounted to 4.42 for T1, 5.64 for T2, 6.90 for T3, 4.93 for Khl, 5.23 for Kh2, 6.18 for Kh3, 6.17 for E1, and 8.48 for E2. Molecular weights of proteinases within each group were close and amounted to 30100 Da for trypsins, 39800 Da for chymotrypsins, and 24000 Da for elastases. The enzymes isolated displayed maximal activities at alkaline pH values. Inhibitor analysis demonstrated that all the proteinases isolated from European catfish pancreas belonged to the serine type.
authors.forename: N N
authors.initials: NN
authors.lastname: Ulitina
authors.forename: V V
authors.initials: VV
authors.lastname: Khabliuk
authors.forename: M T
authors.initials: MT
authors.lastname: Proskuriakov
mesh_terms: D000818:Animals; D002397:Catfishes; D002850:Chromatography, Gel; D007525:Isoelectric Focusing; D010179:Pancreas / Q000201:enzymology*; D012697:Serine Endopeptidases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism
chemical_list: D012697:Serine Endopeptidases