Determination of the complete amino‐acid sequence of porcine miniplasminogen

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Abstract
The complete amino acid sequence of porcine miniplasminogen (MW 37,000), comprising 341 residues, was determined by automated Edman degradation in a liquid-phase or solid-phase sequenator. Selected fragments were produced by cleavage with 2-(2-nitrophenylsulfenyl)-3-methyl-3''-bromoindolenine (BNP-skatole), cyanogen bromide, hydroxylamine, Staphylococcus aureus protease or trypsin or with combinations thereof and by activation with urokinase. The sequence obtained was compared with the known sequences of human and bovine miniplasminogen, indicating that the porcine molecule apparently contains the same structural and functional domains as the protein of the other 2 spp. Porcine miniplasminogen has a sequence homology of 83% with human and of 79% with bovine miniplasminogen; 74% of the aminoa cids are identical in all 3 spp. The results show a higher degree of evolutionary conservatism in the structurally and/or functionally vital regions of the molecule (active site residues, kringle 5).

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