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A propos de cet article
Specific activity:
≥60 Kunitz units/mg solid
Biological source:
bovine pancreas
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Laissez-nous vous aiderSMILES string
[nH]1cnc(c1)CC(NC(=O)CCN)C(=O)O
InChI key
CQOVPNPJLQNMDC-UHFFFAOYSA-N
InChI
1S/C9H14N4O3/c10-2-1-8(14)13-7(9(15)16)3-6-4-11-5-12-6/h4-5,7H,1-3,10H2,(H,11,12)(H,13,14)(H,15,16)
biological source
bovine pancreas
type
Grade XII-S
form
powder
specific activity
≥60 Kunitz units/mg solid
mol wt
13.7 kDa
storage temp.
−20°C
Quality Level
Application
Ribonuclease S from bovine pancreas has been used in a study to assess the hybridase activity of human ribonuclease-1. Ribonuclease S from bovine pancreas has also been used in a study to investigate a new approach to obtaining high-activity RNase, DNase, cholesterolesterase, and trypsin from cattle pancreas.
Other Notes
Protease-modified RNase A
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Classe de stockage
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Beata Schmidt et al.
Journal of chromatography. A, 1018(2), 155-167 (2003-11-19)
The overall topic of the investigation was the separation of basic proteins by cation exchange displacement chromatography. For this purpose two principal column morphologies were compared for the separation of ribonuclease A and alpha-chymotrypsinogen, two proteins found in the bovine
A new approach to obtaining high-activity RNase, DNase, cholesterolesterase, and trypsin from cattle pancreas.
V V Khomov et al.
Doklady. Biochemistry and biophysics, 400, 61-64 (2005-04-26)
Nicoletta Potenza et al.
Nucleic acids research, 34(10), 2906-2913 (2006-06-02)
Human ribonuclease-1 (hRNase-1) is an extracellular enzyme found in exocrine pancreas, blood, milk, saliva, urine and seminal plasma, which has been implicated in digestion of dietary RNA and in antiviral host defense. The enzyme is characterized by a high catalytic
The preparation of subtilisn-modified ribonuclease and the separation of the peptide and protein components.
F M RICHARDS et al.
The Journal of biological chemistry, 234(6), 1459-1465 (1959-06-01)
E Goormaghtigh et al.
European journal of biochemistry, 193(2), 409-420 (1990-10-24)
Attenuated total reflection Fourier-transform infrared spectroscopy of thin hydrated films of soluble and membrane protein included in a phospholipid bilayer is shown to provide useful information as to the secondary structure of the protein. The analysis of the amide I
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