6533b855fe1ef96bd12b10ab
RESEARCH PRODUCT
Aktivität Eiweiss spaltender Enzyme in Fischen
G. Siebertsubject
PharmacologyCathepsinProteasesPh optimumGlycylglycine dipeptidaseCell BiologyBiologyMolecular biologyCellular and Molecular NeuroscienceBiochemistryPeptide HydrolasesMolecular MedicineFish <Actinopterygii>Molecular Biologydescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1958-02-01 | Experientia |