Search results for "Glycylglycine dipeptidase"

showing 2 items of 2 documents

Aktivität Eiweiss spaltender Enzyme in Fischen

1958

Fresh tissues from sea fishes show much higher activities of cathepsins than the corresponding mammalian tissues. The significance of these findings is discussed. There is no indication for the presence in fresh extracts of fish muscle of either proteinases with a pH optimum near neutrality or of decarboxylases for glutamic and aspartic acids. The activities of glycylglycine dipeptidase in fish muscle are found to be at the upper limit of the values obtained by other workers with mammalian tissues.

PharmacologyCathepsinProteasesPh optimumGlycylglycine dipeptidaseCell BiologyBiologyMolecular biologyCellular and Molecular NeuroscienceBiochemistryPeptide HydrolasesMolecular MedicineFish <Actinopterygii>Molecular BiologyExperientia
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Thermische Denaturierung von Kaltblüter-Enzymproteinen

1960

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.

Pharmacologychemistry.chemical_classificationCathepsinGlycylglycine dipeptidaseHeat resistanceCell BiologyCatalysisCellular and Molecular NeuroscienceEnzymeBiochemistrychemistryMolecular MedicineHeat denaturationMolecular BiologyNuclear chemistryExperientia
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