[Ala 2 14,38 ] Aprotinin: Preparation by Partial Desulphurization of Aprotinin by Means of Raney Nickel and Comparison with Other Aprotinin Derivatives

Schnabel, E.; Schröder, W.; Reinhardt, G.

Biological Chemistry Hoppe-Seyler 367(2): 1167-1176

1986


ISSN/ISBN: 0177-3593
DOI: 10.1515/bchm3.1986.367.2.1167
Accession: 067929163

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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.