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product name
Gly-Phe,
化驗
≥97.0% (TLC)
形狀
crystalline
顏色
white
mp
264 °C
儲存溫度
−20°C
SMILES 字串
NCC(=O)N[C@@H](Cc1ccccc1)C(O)=O
InChI
1S/C11H14N2O3/c12-7-10(14)13-9(11(15)16)6-8-4-2-1-3-5-8/h1-5,9H,6-7,12H2,(H,13,14)(H,15,16)/t9-/m0/s1
InChI 密鑰
JBCLFWXMTIKCCB-VIFPVBQESA-N
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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
個人防護裝備
Eyeshields, Gloves, type N95 (US)
Chemistry (Weinheim an der Bergstrasse, Germany), 6(21), 3906-3913 (2000-12-29)
Oligopeptides are efficiently hydrolyzed by Ce(IV) to the corresponding amino acids under mild conditions. The pseudo first-order rate constants for the hydrolysis of H-Gly-Phe-OH and H-Gly-Gly-OH at pH 7.0 and 50 degrees C are 3.5 x 10(-1) and 2.8 x
European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences, 22(5), 399-408 (2004-07-22)
Oil-based depot formulations may constitute a future delivery method for small peptides. Thus, a requirement is attainment of sufficient oil solubility for such active compounds. A model dipeptide (Gly-Phe) has been converted into lipophilic prodrugs by esterification at the C-terminal
Bioscience, biotechnology, and biochemistry, 71(8), 2083-2086 (2007-08-11)
The aim of this study was to improve the performance of affinity gels containing glycyl-D-phenylalanine (Gly-D-Phe) as a ligand to thermolysin. Gly-D-Phe was immobilized to the resin through spacers of varying chain lengths. The resulting affinity gels had spacer chain
Proceedings of the National Academy of Sciences of the United States of America, 103(25), 9512-9517 (2006-06-14)
Natively unfolded phenylalanine-glycine (FG)-repeat domains are alleged to form the physical constituents of the selective barrier-gate in nuclear pore complexes during nucleocytoplasmic transport. Presently, the biophysical mechanism behind the selective gate remains speculative because of a lack of information regarding
The American journal of physiology, 260(3 Pt 2), R563-R569 (1991-03-01)
The transport mechanisms for the dipeptide glycyl-L-phenylalanine (Gly-Phe) and L-phenylalanine (Phe) were characterized in fish intestinal brush-border membrane vesicles (BBMV). Gly-Phe was rapidly hydrolyzed only intravesicularly with almost total hydrolysis occurring even at 10 s. Dipeptide uptake was not stimulated
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