| Autor: |
Sorenson JC; Department of Genetics, North Carolina State University, Raleigh, North Carolina 27650., Scandalios JG |
| Jazyk: |
angličtina |
| Zdroj: |
Plant physiology [Plant Physiol] 1980 Oct; Vol. 66 (4), pp. 688-91. |
| DOI: |
10.1104/pp.66.4.688 |
| Abstrakt: |
Some biochemical properties of the catalase inhibitor purified from maize scutella are described. The inhibitor is heat-labile and its activity is destroyed by trypsin, indicating that it is a protein. It does not appear to be a lectin nor does the inhibition involve proteolysis. The active inhibitor is a dimer with each subunit having a molecular weight of 5600 as determined by sodium dodecyl sulfate electrophoresis. A kinetic analysis performed in the presence of increasing levels of inhibitor gave unusual Lineweaver-Burk patterns. Possible explanations for these patterns are discussed. The inhibitor is active against all catalases tested from a wide variety of organisms. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
|
