推荐产品
化驗
≥95% (LC/MS-ELSD)
形狀
solid
應用
metabolomics
vitamins, nutraceuticals, and natural products
儲存溫度
−20°C
InChI
1S/C21H22O10/c22-8-16-18(26)19(27)20(28)21(31-16)29-11-5-12(24)17-13(25)7-14(30-15(17)6-11)9-1-3-10(23)4-2-9/h1-6,14,16,18-24,26-28H,7-8H2/t14-,16+,18+,19-,20+,21+/m0/s1
InChI 密鑰
DLIKSSGEMUFQOK-SFTVRKLSSA-N
一般說明
Natural product derived from plant source.
訊號詞
Warning
危險聲明
防範說明
危險分類
Aquatic Acute 1 - Aquatic Chronic 1
儲存類別代碼
11 - Combustible Solids
水污染物質分類（WGK）
WGK 3
閃點（°F）
Not applicable
閃點（°C）
Not applicable
J Garcia-Mas et al.
Plant molecular biology, 27(1), 205-210 (1995-01-01)
A number of different cDNA clones corresponding to the most abundant mRNAs present in immature seeds have been isolated from an almond (Prunus amygdalus cv. Texas) immature seed cDNA library. Those corresponding to proteins involved in storage processes have been
J S Choi et al.
Planta medica, 57(3), 208-211 (1991-06-01)
Blood glucose and total lipid levels in rats with streptozotocin-induced diabetes were determined after intraperitoneal administration of a methanolic extract of Prunus davidiana Fr. stems and its main component, prunin (= naringenin 7-O-beta-D-glucoside). From the data obtained it was concluded
K Habelt et al.
Analytical biochemistry, 134(2), 393-397 (1983-10-15)
A naringinase assay capable of distinguishing between the content of naringin, prunin, and naringenin present in the incubation mixture, is described. The amount of these compounds can be estimated by combining two spectrophotometric procedures. (a) Treatment with strong alkali to
LeAnna N Willison et al.
Molecular immunology, 55(3-4), 253-263 (2013-03-19)
Tree nuts are a widely consumed food. Although enjoyed safely by most individuals, allergic reactions to tree nuts, including almond, are not uncommon. Almond prunin (Pru du 6), an 11S globulin (legumin), is an abundant nut seed protein and a
Fernando Soria et al.
Bioscience, biotechnology, and biochemistry, 66(7), 1442-1449 (2002-09-13)
The kinetics of thermal inactivation of A. terreus alpha-rhamnosidase was studied using the substrate p-nitrophenyl alpha-L-rhamnoside between 50 degrees C and 70 degrees C. Up to 60 degrees C the inactivation of the purified enzyme was completely reversible, but samples
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