The induction of collagenase and a neutral proteinase by their high molecular weight substrates in Achromobacter iophagus
| Autor: | B. Keil, R. Misrahi, V. Keil-Dlouha |
|---|---|
| Rok vydání: | 1976 |
| Předmět: |
Achromobacter
Bacterial growth Structural Biology Zymogen medicine Peptide bond Inducer Alcaligenes Molecular Biology chemistry.chemical_classification biology Chemistry Substrate (chemistry) biology.organism_classification Pepsin A Peptide Fragments Molecular Weight Kinetics Microbial Collagenase Enzyme Biochemistry Enzyme Induction Collagenase Collagen Peptide Hydrolases medicine.drug |
| Zdroj: | Journal of Molecular Biology. 107:293-305 |
| ISSN: | 0022-2836 |
| DOI: | 10.1016/s0022-2836(76)80006-x |
| Popis: | The synthesis of collagenase in Achromobacter isophagus has been shown to be inducible by denatured collagen and by its high molecular weight fragments. The presence in the macromolecular inducer of peptide bonds which could be digested by the collagenase is indispensable for the effect of induction. On the other hand, an addition of a low molecular weight substrate or inhibitor of collagenase does not stimulate the enzyme synthesis. Lack of collagenase induction was also observed in the case of β-casein which is a macromolecular substrate with four peptide bonds digestible by the collagenase. Nevertheless in the presence of β-casein the induction of a neutral caseinolytic proteinase was found. The probable role of conformation structure of a macromolecular substrate in the mechanism of induction is discussed. The dependence of induction on the growth phase of the culture was studied. The collagenase activity appears only after the last phase of the exponential growth. It was proved that no zymogen or cell-accumulated enzyme is present in the first stage of exponential growth and that the collagenase synthesis is in direct correlation with a particular state of the bacterial growth cycle. |
| Databáze: | OpenAIRE |
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