Neutral proteinase activity in the human lens
| Autor: | P. Trayhurn, Ruth van Heyningen |
|---|---|
| Rok vydání: | 1976 |
| Předmět: |
Carboxypeptidases
Biology Aminopeptidase Cataract Lens protein Leucyl Aminopeptidase Cellular and Molecular Neuroscience Lens Crystalline medicine Humans Magnesium Protease Inhibitors Edetic Acid chemistry.chemical_classification Neutral proteinase Albumin Hydrogen-Ion Concentration Crystallins Sensory Systems Ophthalmology Protein catabolism Enzyme medicine.anatomical_structure chemistry Biochemistry Lens (anatomy) Calcium Leucine Peptide Hydrolases |
| Zdroj: | Experimental Eye Research. 22:251-257 |
| ISSN: | 0014-4835 |
| DOI: | 10.1016/0014-4835(76)90052-x |
| Popis: | Enzymes associated with protein breakdown have been investigated in the human lens. A neutral proteinase has been found with properties similar to the bovine lens enzyme (Blow, van Heyningen and Barrett, 1975). It is maximally active at pH 7·5, stable for many hours at 55°C, activated by Mg 2+ and Ca 2+ and inhibited by EDTA. It is active against bulk human lens proteins and bovine lens α-crystallin but has little or no activity against haemoglobin, azocasein or bovine plasma albumin. The neutral proteinase appears to be the main, or only, proteinase in the normal and cataractous human lens; we were unable to find the proteinase with maximal activity at pH 5·2 described by Swanson and Nichols (1971). Neither leucine aminopeptidase nor carboxypeptidase A activity could be detected in the human lens. |
| Databáze: | OpenAIRE |
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