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Structure and function of microplasminogen: reconstitution of microplasminogen and microplasmin from isolated fragments.
- Source :
-
Ciba Foundation symposium [Ciba Found Symp] 1997; Vol. 212, pp. 66-76; discussion 76-83. - Publication Year :
- 1997
-
Abstract
- We describe limited chemical proteolysis of microplasminogen/microplasmin (mPlg/mPlm) and their reconstitution from isolated fragments. A V141-->M141 substitution in methionineless human mPlg/mPlm allowed the protein(s) to be cleaved in CNBr/formic acid. The resulting two fragments (141 and 118 residues, respectively), each internally disulfide bonded, were separated by preparative non-reducing gradient SDS-PAGE, and could then be mixed to reconstitute the characteristic mPlg/mPlm, including their activation by urokinase (uPA) and streptokinase (SK), and inhibition by macromolecular inhibitors. The isolated larger, N-terminal fragment, which contains the mPlg activation site in a normal disulfide configuration, was not cleaved by uPA in the absence of its smaller C-terminal companion, showing that the linear amino acid sequence is not by itself sufficient to confer substrate character, even when its conformation is constrained by the disulfide structure.
- Subjects :
- Amino Acid Sequence
Drug Stability
Fibrinolysin physiology
Humans
Molecular Sequence Data
Mutation
Peptide Fragments genetics
Peptide Fragments isolation & purification
Peptide Fragments physiology
Plasminogen antagonists & inhibitors
Plasminogen genetics
Plasminogen physiology
Structure-Activity Relationship
Fibrinolysin chemistry
Peptide Fragments chemistry
Plasminogen chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0300-5208
- Volume :
- 212
- Database :
- MEDLINE
- Journal :
- Ciba Foundation symposium
- Publication Type :
- Academic Journal
- Accession number :
- 9524764
- Full Text :
- https://doi.org/10.1002/9780470515457.ch5