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- W2000273789 abstract "During the activation of human plasminogen by streptokinase (a peptide peptidohydrolase), an acid-soluble fraction is liberated, and its can be collected when the plasmin (EC 3.4.4.14) is precipitated from solution. The total acid-soluble fraction has bee measured as 35–40% of the original preparation of plasminogen. Since this fraction was only partly dialyzablem a peptide portion could be prepared, consisting of the material retained by the dialysis membrane, and containing approximately two-thirds of the acid-soluble fraction. This peptide preparation represented about 25% of the initial protein. The liberated peptide has been named plasminopeptide, and shown to be a mixture of three major components, designated A, B, and C, in decreasing order of electrophoretic mobility at pH 2.0. These plasminopeptides have essentially the same sedimentation coefficient, namely 1.45 S, when corrected to standard conditions and to infinite dilution. Their eletrophoretic mobilities at pH 2.0 are, approx. 6.0·10−5, 4.0·10−5, and 2.0·10−5 cm2 V−1 sec−1. They can be readily separated on columns of Dowex resin, although 0.1 N NaOH is required to elute one of the components." @default.
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- W2000273789 date "1964-05-11" @default.
- W2000273789 modified "2023-09-27" @default.
- W2000273789 title "Molecular changes in the activation of plasminogenI. The release of peptide fragments" @default.
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- W2000273789 doi "https://doi.org/10.1016/0304-4165(64)90058-3" @default.
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