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P5147

Sigma-Aldrich

Protease from Streptomyces griseus

Type XIV, ≥3.5 units/mg solid, powder

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Synonym(s):
Actinase E, Pronase E
CAS Number:
EC Number:
MDL number:
eCl@ss:
32160410

biological source

Streptomyces griseus

Quality Level

type

Type XIV

form

powder

specific activity

≥3.5 units/mg solid

solubility

10 mM NaAc (pH 7.5) and 5 mM CaAc: soluble 0.2 mg/mL at 37 °C, clear, colorless to tan

shipped in

wet ice

storage temp.

−20°C

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This Item
P0652P88117433
Pronase E

7433

Pronase E

form

powder

form

powder

form

powder

form

fine powder

specific activity

≥3.5 units/mg solid

specific activity

≥15 units/mg solid

specific activity

≥3.5 units/mg solid

specific activity

-

solubility

10 mM NaAc (pH 7.5) and 5 mM CaAc: soluble 0.2 mg/mL at 37 °C, clear, colorless to tan

solubility

-

solubility

-

solubility

-

shipped in

wet ice

shipped in

-

shipped in

-

shipped in

ambient

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

Specificity

A mixture of at least three proteolytic activities including an extracellular serine protease. In general, serine proteases display a wide range of substrate specificities, which are believed to be mediated by an active site composed of one Asp, one His, and a Ser residue in the molecule. This enzyme prefers to hydrolyze peptide bonds on the carboxyl side of glutamic or aspartic acid.

Application

Protease from Streptomyces griseus has been used:
  • for the digestion of nucleus pulposus (NP) tissue
  • in the catalysis of asymmetric one pot Mannich reaction
  • for deproteinization of starch
  • digestion of brain slices for the cell dissociation

Protease is an enzyme used to break down proteins by hydrolyzing peptide bonds. Protease is used to degrade proteins, to study protease inhibitors and to study thermal inactivation kinetics. Protease is used in nucleic acid isolation procedures in incubations. Protease from Streptomyces griseus has been used in crystallographic and kinetic investigations of the covalent complex formed by tetrapeptide aldehydes and serine proteases.
Protease is typically used in nucleic acid isolation procedures in incubations of 0.5-3.0 hours supplemented with 0.2% sodium dodecyl sulfate and 10 mM EDTA.
The enzyme from Sigma has been used for the digestion and analysis of antithrombin-heparin complexes. It has also been used for the isolation of enzyme-resistant starch.
This enzyme is more active at a higher pH range than the known alkaline protease, showing the proteolytic activity even in 0.2N NaOH solution. This enzyme is useful for proteolysis of insoluble protein and for structure investigation of protein.

Biochem/physiol Actions

Protease catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Protease from Streptomyces griseus is a mixture of at least three proteolytic activities including an extracellular serine protease. Serine proteases display a wide range of substrate specificities, which are believed to be mediated by an active site composed of one Asp, one His, and a Ser residue in the molecule. This enzyme prefers to hydrolyze peptide bonds on the carboxyl side of glutamic or aspartic acid.
This product is a mixture of at least three caseinolytic activities and one aminopeptidase activity. The caseinolytic enzymes were named as Streptomyces griseus Protease A, Streptomyces griseus Protease B and Streptomyces griseus Trypsin. This product may be used when extensive or complete degradation of protein is required. This protease mixture is highly nonspecific and can digest casein to the extent of >70% as mono-amino acids.

Features and Benefits

  • highly stable in pH range of 5.0 to 9.0, with peak activity at pH 8.8
  • compatible with many DNA and RNA isolation buffers
  • broad substrate specificity

Quality

Contains calcium acetate.

Physical properties

Completely inactivated by heating above 80 °C for 15-20 minutes.

Unit Definition

One unit will hydrolyze casein to produce color equivalent to 1.0 μmole (181 μg) of tyrosine per min at pH 7.5 at 37 °C (color by Folin-Ciocalteu reagent).

Preparation Note

Collected from culture broth of S. griseus.

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Pictograms

Exclamation markHealth hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Customers Also Viewed

Slide 1 of 6

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Protease-catalysed direct asymmetric Mannich reaction in organic solvent
Xue Y, et al.
Scientific reports, 2, 761-761 (2012)
G D Brayer et al.
Proceedings of the National Academy of Sciences of the United States of America, 76(1), 96-100 (1979-01-01)
X-ray crystallographic data show that a specific tetrapeptide aldehyde inhibitor (N-acetylprolylalanylprolylphenylalaninal) forms a stable, covalent, tetrahedral addition complex with the serine protease, SGPA, from Streptomyces griseus. Earlier proposals, based on kinetic measurements, for the covalent nature of such linkages are
An improved fractionation system for pronase on CM-sephadex.
J Jurásek et al.
Canadian journal of biochemistry, 49(11), 1195-1201 (1971-11-01)
A Chan et al.
The Journal of biological chemistry, 272(35), 22111-22117 (1997-08-29)
Although heparin has been used clinically for prophylaxis and treatment of thrombosis, it has suffered from problems such as short duration within compartments in vivo that require long term anticoagulation. A covalent antithrombin-heparin complex has been produced with high anticoagulant
Enzyme-resistant starch. I. Quantitative and qualitative influence of incubation time and temperature of autoclaved starch on resistant starch formation
Eerlingen RC, et al.
Cereal Chem., 70(3), 339-344 (1993)

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