| Autor: |
Gul'nik SV, Yusupova MP, Lavrenova GI, Tartakovsky IS, Prozorovsky SV, Stepanov VM |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of general microbiology [J Gen Microbiol] 1986 Feb; Vol. 132 (2), pp. 387-92. |
| DOI: |
10.1099/00221287-132-2-387 |
| Abstrakt: |
Phenylalanineaminopeptidase was isolated and purified from the culture filtrate of Legionella pneumophila by affinity chromatography on O-tert-butyl-L-threonyl-L-phenylalanyl-L-prolylglycyl-aminosilo chrom and by gel-filtration; a 401-fold purification with a yield of 18% was achieved. The enzyme was a metalloenzyme with a molecular weight of 35000 and a pI of 5.8. It was stable at pH 7-9 and had an activity optimum in the range of pH 8-9.5 with L-phenylalanine p-nitroanilide as substrate. Enzyme activity was highest towards the latter compound, substantially lower towards L-leucine p-nitroanilide and only marginal towards other p-nitroanilides. Besides phenylalanineaminopeptidase, a metalloproteinase and a serine proteinase were also detected in L. pneumophila culture filtrate. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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