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A7550

Sigma-Aldrich

Achromopeptidase from Achromobacter lyticus

lyophilized powder, Protein ~5 % by biuret, 300-600 units/mg solid

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CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204

form

lyophilized powder

specific activity

300-600 units/mg solid

composition

Protein, ~5% biuret

foreign activity

Collagenase, present

storage temp.

−20°C

Biochem/physiol Actions

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.

Unit Definition

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).

Physical form

Crude powder containing salts and medium components

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

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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
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B W Elliott et al.
The Journal of biological chemistry, 261(24), 11259-11265 (1986-08-25)
We report here a procedure which results in the purification of an extracellular protease (designated Ps-1) from Pseudomonas aeruginosa. This enzyme cleaves fibrinogen so that the modified molecules form microcrystals and large single crystals. Precise knowledge of the Ps-1 cleavage
Toshio Tomita et al.
The Journal of biological chemistry, 279(52), 54161-54172 (2004-10-19)
Flammutoxin (FTX), a 31-kDa pore-forming cytolysin from Flammulina velutipes, is specifically expressed during the fruiting body formation. We cloned and expressed the cDNA encoding a 272-residue protein with an identical N-terminal sequence with that of FTX but failed to obtain
High yield preparation of genomic DNA from Streptomyces.
Jasmina Nikodinovic et al.
BioTechniques, 35(5), 932-934 (2003-11-25)

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