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Primary structure of the ‘bait’ region for proteinases in α 2 ‐macroglobulin
Author(s) -
Sottrup-Jensen Lars,
Lønblad Peter B.,
Stepanik Terrence M.,
Petersen Torben E.,
Magnusson Staffan,
Jörnvall Hans
Publication year - 1981
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(81)80197-4
Subject(s) - library science , computer science
Most proteinase inhibitors in blood plasma, e.g., antithromb~.III, Q i-antitrypsin, inter+trypsin inhibitor, are specific towards serine proteinases and form 1 :l complexes engaging the active site and thus completely inhibiting the proteinase activity. a,-Macroglobulin is a tetrameric glycoprote~,~r 725 000, consisting of four app~ently identical chains. ‘Halfmolecules’,Mr 360 000 can be obtained under nonreductive denaturing conditions [ 1,2]. Unlike the other inhibitors (YAM can form complexes with proteinases from different classes having different substrate specificities [3-51. furthermore, the active site of the complexed proteinase is accessible to smaller molecules as shown by the facts that the cr,M-trypsin can cleave synthetic substrates [6] and be inhibited by the bovine pancreatic trypsin inhibitor (Kunitz) (M, 6514) [7]. It. IS not accessible to larger protein substrates or ~hibitors, e.g., soy bean trypsin inhibitor, Mr 20 095 [?I. However, neither zymogens such