title: [Ala214,38]aprotinin: preparation by partial desulphurization of aprotinin by means of Raney nickel and comparison with other aprotinin derivatives.
abstract: Treatment of aprotinin with Raney nickel in the presence or absence of denaturants yielded [Ala2 14,38]aprotinin. Aprotinin and [Ala2 14,38]aprotinin were separated by ion exchange chromatography at pH 8 using CM-Sepharose, fast flow. [Ala2 14,38]aprotinin is a proteinase inhibitor, but it possesses lower affinities than aprotinin, for the enzymes trypsin, alpha-chymotrypsin, pancreatic kallikrein and plasmin as reflected by higher Ki values [Ala2 14,38]aprotinin is slowly degraded by trypsin. The optical activity of [Ala2 14,38]aprotinin in different solvents is quite similar to that of aprotinin, or that of its hydrolysis products, [seco-15/16]aprotinin or [di-seco-15/16,39/40]-aprotinin. This is taken as good evidence for analogous molecular conformations of all these substances.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D007611:Aprotinin / Q000302:isolation & purification*; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D007202:Indicators and Reagents; D007700:Kinetics; D009532:Nickel; D011048:Polarography; D013455:Sulfur; D013552:Swine; D014357:Trypsin
chemical_list: D007202:Indicators and Reagents; D013455:Sulfur; D009532:Nickel; D007611:Aprotinin; D014357:Trypsin