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Merck
CN

83553

Rennin from Mucor miehei

lyophilized, powder, slightly brown, ~0.1 U/mg

别名:

Mucorpepsin

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关于此项目

化学文摘社编号:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-975-5
MDL number:
Specific activity:
~0.1 U/mg
Biological source:
fungus (Mucor miehei)
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biological source

fungus (Mucor miehei)

form

powder

quality

lyophilized

specific activity

~0.1 U/mg

color

slightly brown

storage temp.

−20°C

Other Notes

1 U corresponds to the amount of enzyme which liberates 1 μmol folin-positive amino acids and peptides (calculated as tyrosine) per minute at pH 7.5 and 37°C (casein, Cat. No. 22078, as substrate)
Action on a synthetic chromophoric hexapeptide
Sales restrictions may apply

pictograms

Health hazardExclamation mark

signalword

Danger

Hazard Classifications

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

target_organs

Respiratory system

存储类别

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Faceshields, Gloves

法规信息

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分析证书(COA)

Lot/Batch Number

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Bond specificity, active site and milk clotting mechanism of the Mucor miehei protease.
M Sternberg
Biochimica et biophysica acta, 285(2), 383-392 (1972-12-28)
Hongyan Sun et al.
Biopolymers, 88(2), 141-149 (2007-01-09)
We have successfully developed a protease assay using fluorescence resonance energy transfer based peptide libraries, which allows not only general detection of enzymatic activities, but more importantly substrate fingerprinting of proteases from different classes. The method allows the generation of
P Martin et al.
Biochimica et biophysica acta, 612(2), 410-420 (1980-04-11)
The action of two milk-clotting fungal proteases from Mucos pusillus and Mucor miehei and of chymosins A and B on the hexapeptide, Leu-Ser-Phe(NO2)-Nle-Ala-Leu-OMe, and on kappa-casein were studied. The effects of pH and temperature on the initial rates of hydrolysis
M Baudys et al.
FEBS letters, 235(1-2), 271-274 (1988-08-01)
The amino acid sequence of Mucor pusillus aspartic proteinase was determined by analysis of fragments obtained from cleavage of the enzyme by CNBr and limited tryptic digestion. The proteinase is a single polypeptide chain protein containing 361 amino acid residues

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