A7550
Achromopeptidase from Achromobacter lyticus
lyophilized powder, Protein ~5 % by biuret, 300-600 units/mg solid
表单
lyophilized powder
比活
300-600 units/mg solid
组成
Protein, ~5% biuret
异质活性
Collagenase, present
储存温度
−20°C
生化/生理作用
Achromopeptidase is a lysyl endopeptidase with a MW of ~27 kDa. It is useful for lysis of Gram-positive bacteria that are resistant to lysozyme.
pH Optimum for activity: pH 8.5 - 9
Approximately 500-1,500 un/ml achromopetidase can be used to lyse cells at a density of OD600=0.6 over 2 hours at 37 °C.
pH Optimum for activity: pH 8.5 - 9
Approximately 500-1,500 un/ml achromopetidase can be used to lyse cells at a density of OD600=0.6 over 2 hours at 37 °C.
外形
Crude powder containing salts and medium components
其他说明
One unit will produce a change in A600 of 0.001 per minute per mL at pH 8.0 at 37 °C using a suspension of Micrococcus lysodeikticus as substrate (1 cm light path).
警示用语：
Danger
危险声明
预防措施声明
危险分类
Resp. Sens. 1
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
法规信息
新产品
此项目有
Niamh Toomey et al.
Applied and environmental microbiology, 75(10), 3146-3152 (2009-03-10)
Three wild-type dairy isolates of lactic acid bacteria (LAB) and one Lactococcus lactis control strain were analyzed for their ability to transfer antibiotic resistance determinants (plasmid or transposon located) to two LAB recipients using both in vitro methods and in
Beatrice Quevedo et al.
BMC microbiology, 11, 14-14 (2011-01-21)
The purpose of this study was to design and evaluate fluorescent in situ hybridization (FISH) probes for the single-cell detection and enumeration of lactic acid bacteria, in particular organisms belonging to the major phylogenetic groups and species of oral lactobacilli
Jian Zhang et al.
Journal of chromatography. A, 1154(1-2), 295-307 (2007-04-20)
This paper describes approaches to optimize the chromatographic performance for our recently developed LC-MS platform, extended range proteomic analysis (ERPA), for comprehensive protein characterization at the ultratrace level. Large digested peptide fragments up to 10 kDa (e.g., from lysyl endopeptidase
Krzysztof Regulski et al.
PloS one, 7(2), e32301-e32301 (2012-03-03)
Peptidoglycan (PG) is the major component of Gram positive bacteria cell wall and is essential for bacterial integrity and shape. Bacteria synthesize PG hydrolases (PGHs) which are able to cleave bonds in their own PG and play major roles in
S Tsunasawa et al.
The Journal of biological chemistry, 264(7), 3832-3839 (1989-03-05)
The complete amino acid sequence of Achromobacter lyticus protease I (EC 3.4.21.50), which specifically hydrolyzes lysyl peptide bonds, has been established. This has been achieved by sequence analysis of the reduced and S-carboxymethylated protease and of peptides obtained by enzymatic
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