Beteiligte Stoffe
| Rolle | Name | HCID | Einwaage |
|---|
| Edukt | Acetate | HCID 175 | — |
| Edukt | L-Lysine | HCID 5962 | — |
| Edukt | Potassium Phosphate, Tribasic | HCID 62657 | — |
| Edukt | 3-Methyl-2-benzothiazolinone hydrazone hydrochloride | HCID 78041 | — |
| Produkt | 6-Amino-2-oxohexanoic acid | HCID 439954 | — |
Reaktionsschritte
The activity of the present enzyme was measured in accordance with Soda's method (Analytical Biochemistry Vol. 25, p. 228, 1968) in the following manner. A reaction mixture consisting of 0.7 ml of 0.1 M potassium phosphate buffer (pH 8.0), 0.1 ml of catalase (750 U/ml), 0.1 ml of 0.1 M L-lysine solution and 0.1 ml of the present enzyme solution was incubated at 37° C. for 20 minutes with gentle shaking. After the incubation the reaction was terminated by the addition of 0.1 ml of 25% trichloroacetic acid. To the resulting reaction mixture were added 1.9 ml of 1 M acetate buffer (pH 5.0) and 0.8 ml of 0.1% 3-methyl-2-benzothiazolone hydrazone hydrochloride solution. The mixture was further incubated at 30° C. for 30 minutes and then allowed to cool to room temperature, after which measurement of optical density at 318 nm was carried out. The formed α-keto-ε -aminocaproic acid thus formed was determined from the resulting calibration curve. One unit of the enzyme was defined as the quantity of the enzyme catalyzing the formation of 1 μmol of α-keto-ε-aminocaproic acid at 37° C. per minute. The relative activity of the enzyme was also assayed by manometric and polarographic determination of the oxygen consumption.
Herkunft & Nachweise
| DOI | 10.6084/m9.figshare.5104873.v1 |
|---|
| Patentnummer | US04234691 |
|---|
| Quelldatensatz | uspto-grants-1980_11 |
|---|
| ORD ID | ord-cf1a7cc260784b448642a5e80cbf8003 |
|---|
| Quellennotiz | uspto-grants-1980_11 |
|---|