추천 제품
Quality Level
분석
≥95%
형태
powder
저장 온도
−20°C
SMILES string
Cl[H].CC1Nc2nc(N)nc(O)c2NC1C
InChI
1S/C8H13N5O.ClH/c1-3-4(2)11-6-5(10-3)7(14)13-8(9)12-6;/h3-4,10H,1-2H3,(H4,9,11,12,13,14);1H
InChI key
GIHYTRGUZVYCQX-UHFFFAOYSA-N
생화학적/생리학적 작용
Synthetic reduced pterin cofactor for nitric oxide synthetase, and for phenylalanine, tyrosine, and tryptophan hydroxylases; less active than the natural cofactor, tetrahydrobiopterin (BH4).
신호어
Danger
유해 및 위험 성명서
Hazard Classifications
Eye Dam. 1 - Skin Irrit. 2 - STOT SE 3
표적 기관
Respiratory system
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
가장 최신 버전 중 하나를 선택하세요:
시험 성적서(COA)
이미 열람한 고객
Proceedings of the National Academy of Sciences of the United States of America, 88(13), 5734-5738 (1991-07-01)
A monoclonal anti-idiotype antibody, NS7, previously shown to mimic the binding of the pterin cofactor of phenylalanine hydroxylase (phenylalanine 4-monooxygenase, EC 1.14.16.1) has been used to localize the cofactor binding site within the phenylalanine hydroxylase catalytic domain to a 27-amino-acid
Biochimica et biophysica acta, 789(2), 111-118 (1984-09-11)
A new microbial inhibitor for rat-liver phenylalanine hydroxylase (L-phenylalanine, tetrahydropteridine: oxygen oxidoreductase (4-hydroxylating), EC 1.14.16.1) was isolated from a culture medium of Fomes tasmanicus, and its structure was determined as 3,4-dihydroxystyrene. This compound inhibited the enzyme by 50% at a
Journal of biochemistry, 90(2), 567-569 (1981-08-01)
A simple and rapid method for isolating tryptophan 5-monooxygenase [L-tryptophan, tetrahydropteridine:oxygen oxidoreductase (5-hydroxylating), EC 1.14.16.4] was reported. The method involves adsorption on calcium phosphate gel and affinity chromatography on agarose coupled with dimethyltetrahydropteridine. Tryptophan 5-monooxygenase was purified 1,100-fold from a
Acta physiologica et pharmacologica latinoamericana : organo de la Asociacion Latinoamericana de Ciencias Fisiologicas y de la Asociacion Latinoamericana de Farmacologia, 34(3), 235-243 (1984-01-01)
Cholinergic modulation on the regulation of tyrosine hydroxylase was studied in guinea pig atria depolarized with high potassium concentration. In these conditions there was an increment in tyrosine hydroxylase activity as well as in the release of radioactivity from atria
The Journal of biological chemistry, 263(3), 1223-1230 (1988-01-25)
The pH optimum of rat liver phenylalanine hydroxylase is dependent on the structure of the cofactor employed and on the state of activation of the enzyme. The tetrahydrobiopterin-dependent activity of native phenylalanine hydroxylase has a pH optimum of about 8.5.
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