Application
L-Tyrosine decarboxylase from Streptococcus faecalis has been used in a study to isolate and identify the carbonyl-active site of diamine oxidase by gas chromatographic mass spectrometry. L-Tyrosine decarboxylase from Streptococcus faecalis has also been used in a study to investigate the adsorption of Streptococcus faecalis on diatomite carriers for use in biotransformations.
Other Notes
Dried cells from which activity can be extracted.
One unit will cause the decomposition of 1.0 μmole of L-tyrosine per min at pH 6.2 at 37 °C.
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
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相关内容
QC Methods
F Buffoni
Analytical biochemistry, 220(1), 185-191 (1994-07-01)
An adduct with phenylhydrazine was formed with the purified pig kidney diamine oxidase and in parallel with the l-tyrosine decarboxylase from Streptococcus faecalis. The labeled enzymes were hydrolyzed by chemical hydrolysis and the adducts released by hydrolysis were isolated and
Characterization of bacterial L-(-)-tyrosine decarboxylase by isoelectric focusing and gel chromatography
Allenmark, C. and B. Servenius
Journal of Chromatography A, 153, 238-245 (1978)
W A Anderson et al.
Journal of chemical technology and biotechnology (Oxford, Oxfordshire : 1986), 47(2), 93-100 (1990-01-01)
Adsorption of cells on particulate carriers is potentially one of the most cost-effective immobilization techniques available. Diatomite carriers, such as Celite, have desirable physical properties, are inexpensive, and are suitable for both mycelial and bacterial systems. This work investigated the
全球贸易项目编号
| 货号 | GTIN |
|---|---|
| T7677-10UN | 04061833632444 |