Collagenase activity in homogenates of the involuting rat uterus
| Autor: | Janet N. Ryan, J. Frederick Woessner |
|---|---|
| Rok vydání: | 1973 |
| Předmět: |
Cations
Divalent Uterus Peptide Divalent Structure-Activity Relationship Pregnancy medicine Animals Chelation Cysteine Edetic Acid Chelating Agents Mercaptoethanol chemistry.chemical_classification Temperature General Medicine Hydrogen-Ion Concentration Rats Enzyme Activation Microbial Collagenase medicine.anatomical_structure Enzyme chemistry Biochemistry Collagenase Calcium Female Peptides Digestion Subcellular Fractions medicine.drug |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Enzymology. 309:397-405 |
| ISSN: | 0005-2744 |
| DOI: | 10.1016/0005-2744(73)90038-7 |
| Popis: | Collagenase activity can be detected in the 6000 × g pellets of homogenates of the involuting uterus of the rat; it digests the collagen present in the homogenates. This enzyme appears to be identical to the collagenase obtained from cultures of uterine tissue. The enzyme is optimally active at pH 7.5, requires Ca2+ (0.01 M) for activity and is inhibited by EDTA and other chelating agents. EDTA inhibition cannot be reversed by adding excess Ca2+ or other divalent cations. The activity is inhibited by the tissue supernatant and by rat serum in 1:100 dilution. The enzyme is insensitive to 1 mM cysteine but is inhibited by other reducing agents such as 1 mM mercaptoethanol. The enzyme does not digest the peptide phenylazobenzyloxycarbonyl-Pro-Leu-Gly- Pro-d-Arg which is used for the assay of bacterial collagenase. The enzyme attacks insoluble collagen at 30°C but does not release digestion products unless the temperature is raised to 37°C. The digestion products at 37°C are smaller than 100 000 daltons and about one-third is diffusible. |
| Databáze: | OpenAIRE |
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