A1057
L-Aspartic acid β-(7-amido-4-methylcoumarin)
≥98%, suitable for ligand binding assays
동의어(들):
L-Aspartic acid β-(4-methyl-7-coumarinylamide), L-Aspartic acid 4-(4-methyl-7-coumarinylamide)
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모든 사진(1)
About This Item
실험식(Hill 표기법):
C14H14N2O5
CAS Number:
Molecular Weight:
290.27
MDL number:
UNSPSC 코드:
12352209
PubChem Substance ID:
NACRES:
NA.26
추천 제품
제품명
L-Aspartic acid β-(7-amido-4-methylcoumarin), fluorescent amino acid
Quality Level
분석
≥98%
양식
powder
기술
ligand binding assay: suitable
색상
white to off-white
저장 온도
−20°C
SMILES string
CC1=CC(=O)Oc2cc(NC(=O)C[C@H](N)C(O)=O)ccc12
InChI
1S/C14H14N2O5/c1-7-4-13(18)21-11-5-8(2-3-9(7)11)16-12(17)6-10(15)14(19)20/h2-5,10H,6,15H2,1H3,(H,16,17)(H,19,20)/t10-/m0/s1
InChI key
ARZPQBJTLVVDNP-JTQLQIEISA-N
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생화학적/생리학적 작용
L-Aspartic acid β-(7-amido-4-methylcoumarin) is used as a fluorogenic substrate for studying the specificity and kinetics of lysosomal glycoasparaginase(s) (aspartylglucosaminidase) and L-asparaginase(s).
L-Aspartic acid-β-7-amido-4-methylcoumarin is sensitive and specific fluorogenic substrate used to assay for lysosomal glycoasparaginase (aspartylglucosaminidase) activity and the diagnosis of aspartylglucosaminuria.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
개인 보호 장비
Eyeshields, Gloves, type N95 (US)
P Ylikangas et al.
Analytical biochemistry, 280(1), 42-45 (2000-05-11)
The antineoplastic enzyme L-asparaginase is commonly used for the induction of remission in acute lymphoblastic leukemia (ALL). There is no simple method available for measuring the activity of this highly toxic drug. We incubated L-asparaginase from Erwinia chrysanthemi with L-aspartic
I T Mononen et al.
Analytical biochemistry, 208(2), 372-374 (1993-02-01)
Recent experimental work on the mechanism of action of glycosylasparaginase suggests that the enzyme specifically reacts toward the L-asparagine or L-aspartic acid moiety of its substrates. Based on this, a new sensitive assay for glycosylasparaginase activity has been developed using
I Mononen et al.
Clinical chemistry, 40(3), 385-388 (1994-03-01)
Serum, plasma, and lymphocytes from aspartylglycosaminuria (AGU) patients and carriers and from normal controls were incubated with a fluorescent glycosylasparaginase substrate, L-aspartic acid beta-(7-amido-4-methylcoumarin), and the release of 7-amino-4-methylcoumarin was measured fluorometrically after incubation for 1-4 h. The mean glycosylasparaginase
Seiji Saito et al.
Biochemical and biophysical research communications, 377(4), 1168-1172 (2008-11-11)
To elucidate the basis of aspartylglucosaminuria (AGU) from the viewpoint of enzyme structure, we constructed structural models of mutant aspartylglucosaminidase (AGA) proteins using molecular modeling software, TINKER. We classified the amino acid substitutions responsible for AGU and divided them into
Voznyi YaV et al.
Journal of inherited metabolic disease, 16(6), 929-934 (1993-01-01)
L-Aspartic acid-beta-7-amido-4-methylcoumarin is a sensitive and specific fluorogenic substrate for lysosomal glycoasparaginase (aspartylglucosaminidase). Fibroblasts and leukocytes from 8 patients with aspartylglucosaminuria, showed 1-7% of the mean normal glycoasparaginase activity. Heterozygotes showed intermediate activities. Glycoasparaginase activity in chorionic villi, cultured trophoblasts
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