89064
4-Phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-D-Arg -trifluoracetat (Salz)
collagenase substrate, chromogenic, ≥95% (HPLC), powder
Synonym(e):
Pz-Pro-Leu-Gly-Pro-D-Arg -trifluoracetat (Salz)
Anmeldenzur Ansicht organisationsspezifischer und vertraglich vereinbarter Preise
Alle Fotos(1)
About This Item
Empirische Formel (Hill-System):
C38H52N10O8 · xC2HF3O2
Molekulargewicht:
776.88 (free base basis)
UNSPSC-Code:
12352204
NACRES:
NA.32
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product name
4-Phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-D-Arg -trifluoracetat (Salz), ≥95% (HPLC)
Assay
≥95% (HPLC)
Form
powder
Anwendung
geeignet als Kollagenase-Substrat
Verpackung
Bottomless glass bottle. Contents are inside inserted fused cone.
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Analysenzertifikate (COA)
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Highly sensitive assay for PZ-peptidase activity by high-performance liquid chromatography
Chikuma, T., et al.
Journal of Chromatography A, 348, 205-212 (1985)
T Chikuma et al.
Journal of chromatography, 635(1), 81-87 (1993-04-09)
A rapid and sensitive assay method for the determination of PZ-peptidase activity is reported. This method is based on the monitoring of the absorption at 320 nm of 4-phenylazobenzyloxycarbonyl-L-Pro-L-Leu (PZ-Pro-Leu), enzymatically formed from the substrate 4-phenylazobenzyloxycarbonyl-L-Pro-L-Leu-Gly-L-Pro-D-Arg (PZ-peptide), after separation by
A Study of the Collagen-binding Domain of a 116-kDaClostridium histolyticum Collagenase*
Osamu Matsushita
The Journal of Biological Chemistry (1998)
U Tisljar
Biological chemistry Hoppe-Seyler, 374(2), 91-100 (1993-02-01)
Thimet oligopeptidase (EC 3.4.24.15) is a thiol-dependent metallo-endopeptidase also known as Pz-peptidase, collagenase-like peptidase, endooligopeptidase A, soluble metallo-endopeptidase and endopeptidase 24.15. The enzyme is closely related to the yeast proteinase yscD. Thimet oligopeptidase (M(r) 74000) is widely distributed in animals
C H Evans
The Biochemical journal, 195(3), 677-684 (1981-06-01)
Tervalent cations of the lanthanide (rare-earth) elements reversibly inhibit bacterial collagenase (clostridiopeptidase A; EC 3.4.24.3). Sm(3+), whose ionic radius is closest to that of Ca(2+), is the most effective inhibitor, completely suppressing clostridiopeptidase activity at a concentration of 100mum in
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