6533b858fe1ef96bd12b627b
RESEARCH PRODUCT
Thermische Denaturierung von Kaltblüter-Enzymproteinen
A. SchmittG. SiebertR. V. MalortieE. Adloffsubject
Pharmacologychemistry.chemical_classificationCathepsinGlycylglycine dipeptidaseHeat resistanceCell BiologyCatalysisCellular and Molecular NeuroscienceEnzymeBiochemistrychemistryMolecular MedicineHeat denaturationMolecular BiologyNuclear chemistrydescription
The temperature, which leads to 50% reduction of catalytic activity by heat denaturation, has been determined for 8 different enzymes from cod muscle, as being in the range between 30 and 52°C. Therefore, there are no indications of a generally different heat resistance of enzymes from cold-blooded animals as compared with those from warm-blooded animals. The same conclusion is derived from calculations ofQ10-values, measured between +37 and − 37°C for cathepsin and glycylglycine dipeptidase.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1960-11-01 | Experientia |