ChemicalBook--->CAS DataBase List--->9031-96-3

9031-96-3

9031-96-3 Structure

9031-96-3 Structure
IdentificationBack Directory
[Name]

PEPTIDASE
[CAS]

9031-96-3
[Synonyms]

EREPSIN
Ereptase
PEPTIDASE
Peptidases
Peptidase A
Exoprotease
Exopeptidase
Sumizyme FLAP
Polypeptidase
EREPSIN EX HOG
Sumizyme LP-20
Pandidase NP-2
Neuropeptidase
FlavorPro 750P
Flavorpro 192P
PEPTIDASE EX HOG
Sternzyme B15024
Sternzym BP 5200
Peptide hydrolase
FlavorPro Whey 750P
Native Porcine Peptidase
Hydroxide peptide hydrolase
peptidase from porcine intestinal*mucosa
PEPTIDASE TBL-1 (ACHROMOPEPTIDASE) FROM ACHROMOBACTER LYTICUS M497-1 ACTIVITY: 1,000 UNITS MG
PEPTIDASE TBL-1 (ACHROMOPEPTIDASE) FROM ACHROMOBACTER LYTICUS M497-1 ACTIVITY: 10,000-20,000 UNITS MG.
[EINECS(EC#)]

232-875-1
[MDL Number]

MFCD00131827
Chemical PropertiesBack Directory
[storage temp. ]

2-8°C
[form ]

powder
[color ]

light brown
[EPA Substance Registry System]

Peptidase (9031-96-3)
Safety DataBack Directory
[Symbol(GHS) ]

Health Hazard (GHS08)
GHS08
[Signal word ]

Danger
[Hazard statements ]

H334
[Precautionary statements ]

P261-P285-P304+P341-P342+P311-P501
[Hazard Codes ]

Xn
[Risk Statements ]

36/37/38-42
[Safety Statements ]

22-24-26-36/37
[WGK Germany ]

1
[RTECS ]

UK9540000
[F ]

10
[TSCA ]

TSCA listed
Hazard InformationBack Directory
[Uses]

Peptidase (IMPa) (Erepsin) is catalytically active enzyme that cleaves peptide bonds in proteins and peptides by hydrolysis[1].
[Purification Methods]

The dipeptidase is purified 700-fold by homogenising the tissue, extracting with Triton X-100, elimination of insoluble material, and ion-exchange, size exclusion and affinity chromatography. [Hitchcock et al. Anal Biochem 163 219 1987.] Restriction enzymes (endonucleases). These are enzymes which cleave double-stranded DNA (linear or circular) at specific nucleotide sequences within the DNA strands which are then used for cloning (by ligating bits of DNA sequences together) or for identifying particular DNA materials, e.g. plasmids, genes etc. A very large number of restriction enzymes are now available commercially and are extensively used in molecular biology. They are highly specific for particular nucleotide arrangements and are sensitive to the reaction conditions, e.g. composition of the medium, pH, salt concentration, temperature etc, which have to be strictly adhered to. Endonucleases are essentially of two types. One type cleaves the DNA producing blunt ends, i.e. the nucleotides are paired at each end. The second type cleaves the DNA leaving hanging ends, i.e. the nucleotides at the ends of each strand (usually four nucleotides) of the double strands protrude ahead of the paired nucleotides. The latter enzymes particularly allow ligation of the cleaved sequence to occur in a desired direction. The enzymes do not require further purification, and the reaction conditions are also provided by the suppliers from which the necessary reaction media can also be purchased (see commercial catalogues).
[References]

[1] Nguyen TTH, et, al. Distributions of Extracellular Peptidases Across Prokaryotic Genomes Reflect Phylogeny and Habitat. Front Microbiol. 2019 Mar 5;10:413. DOI:10.3389/fmicb.2019.00413
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