Reaction of proteinases with alpha 2-macroglobulin: evidence for alternate reaction pathways in the inhibition of trypsin.

Biochemistry
L J LarssonD K Strickland

Abstract

Titration experiments were employed to measure the binding stoichiometry of alpha 2M for trypsin at high and low concentrations of reactants. These titration experiments were performed by measuring the SBTI-resistant trypsin activity and by direct binding measurements using 125I-labeled trypsin. The binding stoichiometry displayed a marked dependence upon protein concentration. At high alpha 2M concentrations (micromolar), 2 mol of trypsin are bound/mol of inhibitor. However, at low alpha 2M concentrations (e.g., 0.5 nM), only 1.3 mol of trypsin were bound/mol of inhibitor. Sequential additions of subsaturating amounts of trypsin to a single aliquot of alpha 2M also resulted in a reduction in the final binding ratio. A model has been formulated to account for these observations. A key element of this model is the observation that purified 1:1 alpha 2M-proteinase complexes are not capable of binding a full mole of additional proteinase [Strickland et al. (1988) Biochemistry 27, 1458-1466]. The model predicts that once the 1:1 alpha 2M-proteinase complex forms, this species undergoes a time-dependent conformational rearrangement to yield a complex with greatly reduced proteinase binding ability. According to this model, the abili...Continue Reading

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Citations

Jan 1, 1994·The International Journal of Biochemistry·F Van JaarsveldJ Travis
Jan 1, 1992·Electron Microscopy Reviews·E DelainF Van Leuven
Sep 10, 1994·Annals of the New York Academy of Sciences·L Sottrup-Jensen
Feb 21, 2002·Proceedings of the National Academy of Sciences of the United States of America·Hiroshi OiMasatoshi Noda
Sep 10, 1994·Annals of the New York Academy of Sciences·R D Feinman

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