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Alpha-2-plasmin inhibitor comprises a single domain
- Source :
- Biochemical and biophysical research communications. 139(3)
- Publication Year :
- 1986
-
Abstract
- The reaction between plasmin and alpha 2PI (alpha-2-plasmin inhibitor), which constitutes a major regulatory step in fibrinolysis, involves both interactions between the kringle structures of plasmin and a complementary site on the inhibitor, and also between the inhibitor reactive center and the enzyme active site. An attempt was made to distinguish calorimetrically the two functional domains of alpha 2PI. Only one transition was seen, both in the DSC and UV experiments, contrary to the expected two. This transition was unaffected by K4 of plasminogen but was abolished in the presence of anhydrotrypsin. This suggests the major domain structure in alpha 2PI is associated with the reactive center.
- Subjects :
- Plasmin
Stereochemistry
Ultraviolet Rays
medicine.medical_treatment
Biophysics
Alpha (ethology)
Biochemistry
chemistry.chemical_compound
Fibrinolysis
medicine
Humans
Fibrinolysin
Molecular Biology
Reactive center
Polyacrylamide gel electrophoresis
HEPES
alpha-2-Antiplasmin
Binding Sites
biology
Transition (genetics)
Calorimetry, Differential Scanning
Chemistry
Active site
Cell Biology
biology.protein
medicine.drug
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 139
- Issue :
- 3
- Database :
- OpenAIRE
- Journal :
- Biochemical and biophysical research communications
- Accession number :
- edsair.doi.dedup.....62d3561c2af4482cfaba3f42994d19a7