Selective inhibition of elastolytic and proteolytic properties of elastase
The elastolytic and proteolytic (fibrin, casein, and hemoglobin) properties of elastase, purified by CM-cellulose chromatography and electrophoretically homogeneous at pH's 9.0 and 4.5, could be selectively inhibited. Soybean trypsin inhibitor and kallikrein inactivator substantially suppressed...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 1962-08, Vol.98 (2), p.191-196 |
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| container_end_page | 196 |
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| container_title | Archives of biochemistry and biophysics |
| container_volume | 98 |
| creator | Walford, Roy L. Kickhöfen, Botho |
| description | The elastolytic and proteolytic (fibrin, casein, and hemoglobin) properties of elastase, purified by CM-cellulose chromatography and electrophoretically homogeneous at pH's 9.0 and 4.5, could be selectively inhibited. Soybean trypsin inhibitor and kallikrein inactivator substantially suppressed proteolytic activity of the enzyme, but were without influence on its elastolytic properties. Conversely, elastolysis was substantially suppressed by high molar salt concentration, whereas proteolysis was not influenced thereby. These results suggest either the presence of several enzymes with similar chromatographic and electrophorctic properties, or else that elastase has more than one active center, one directed against as yet unspecified regions or linkages of elastin, the other having broad and more classical proteolytic properties. |
| doi_str_mv | 10.1016/0003-9861(62)90172-8 |
| format | Article |
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Soybean trypsin inhibitor and kallikrein inactivator substantially suppressed proteolytic activity of the enzyme, but were without influence on its elastolytic properties. Conversely, elastolysis was substantially suppressed by high molar salt concentration, whereas proteolysis was not influenced thereby. 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Soybean trypsin inhibitor and kallikrein inactivator substantially suppressed proteolytic activity of the enzyme, but were without influence on its elastolytic properties. Conversely, elastolysis was substantially suppressed by high molar salt concentration, whereas proteolysis was not influenced thereby. 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Soybean trypsin inhibitor and kallikrein inactivator substantially suppressed proteolytic activity of the enzyme, but were without influence on its elastolytic properties. Conversely, elastolysis was substantially suppressed by high molar salt concentration, whereas proteolysis was not influenced thereby. These results suggest either the presence of several enzymes with similar chromatographic and electrophorctic properties, or else that elastase has more than one active center, one directed against as yet unspecified regions or linkages of elastin, the other having broad and more classical proteolytic properties.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>14004552</pmid><doi>10.1016/0003-9861(62)90172-8</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Archives of biochemistry and biophysics, 1962-08, Vol.98 (2), p.191-196 |
| issn | 0003-9861 1096-0384 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_83141883 |
| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Hydrolases Old Medline Pancreatic Elastase Protease Inhibitors Proteolysis Serine Endopeptidases |
| title | Selective inhibition of elastolytic and proteolytic properties of elastase |
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