Synthesis of potent CXCR4 inhibitors possessing low cytotoxicity and improved biostability based on T140 derivativesElectronic supplementary information (ESI) available: Fig. S1: behaviors of TE14005 (a), TE14011 and Ac-TE14011 (b) in mouse serum; Fig. S2: behaviors of TE14011 (a), Ac-TE14011 (b), TN14003 (c), Ac-TN14003 (d), TC14012 (e) and Ac-TC14012 (f) in rat liver homogenate; Table S1: characterization data of novel synthetic peptides; HPLC charts for synthetic compounds of TE14005, TE14011 and Ac-TE14011, and for a degraded sample of TE14011 in rat liver homogenate and its co-injection with an authentic compound des-[Arg1, Arg2, Nal3]-TE14011. See http://www.rsc.org/suppdata/ob/b3/b306473p/

2003 ◽  
Vol 1 (21) ◽  
pp. 3656 ◽  
Author(s):  
Hirokazu Tamamura ◽  
Kenichi Hiramatsu ◽  
Shuichi Kusano ◽  
Shigemi Terakubo ◽  
Naoki Yamamoto ◽  
...  
Keyword(s):  
Rat Liver ◽  
Synthetic Peptides ◽  
Liver Homogenate ◽  
Supplementary Information ◽  
Mouse Serum ◽  
Synthetic Compounds ◽  
Authentic Compound ◽  
Low Cytotoxicity

scholarly journals Biotransformation of Timosaponin BII into Seven Characteristic Metabolites by the Gut Microbiota

Molecules ◽  
2021 ◽  
Vol 26 (13) ◽  
pp. 3861
Author(s):  
Guo-Ming Dong ◽  
Hang Yu ◽  
Li-Bin Pan ◽  
Shu-Rong Ma ◽  
Hui Xu ◽  
...  
Keyword(s):  
Gut Microbiota ◽  
Rat Liver ◽  
Pharmacological Activity ◽  
Liver Homogenate ◽  
Intestinal Flora ◽  
Important Indicator ◽  
Metabolic Characteristics ◽  
Metabolic Behavior ◽  
First Time ◽  
Rat Liver Microsome

Timosaponin BII is one of the most abundant Anemarrhena saponins and is in a phase II clinical trial for the treatment of dementia. However, the pharmacological activity of timosaponin BII does not match its low bioavailability. In this study, we aimed to determine the effects of gut microbiota on timosaponin BII metabolism. We found that intestinal flora had a strong metabolic effect on timosaponin BII by HPLC-MS/MS. At the same time, seven potential metabolites (M1-M7) produced by rat intestinal flora were identified using HPLC/MS-Q-TOF. Among them, three structures identified are reported in gut microbiota for the first time. A comparison of rat liver homogenate and a rat liver microsome incubation system revealed that the metabolic behavior of timosaponin BII was unique to the gut microbiota system. Finally, a quantitative method for the three representative metabolites was established by HPLC-MS/MS, and the temporal relationship among the metabolites was initially clarified. In summary, it is suggested that the metabolic characteristics of gut microbiota may be an important indicator of the pharmacological activity of timosaponin BII, which can be applied to guide its application and clinical use in the future.

scholarly journals Synthetic peptides including acidic clusters as substrates and inhibitors of rat liver casein kinase TS (type-2).

1984 ◽  
Vol 259 (23) ◽  
pp. 14576-14579 ◽  
Author(s):  
F Meggio ◽  
F Marchiori ◽  
G Borin ◽  
G Chessa ◽  
L A Pinna
Keyword(s):  
Rat Liver ◽  
Synthetic Peptides ◽  
Casein Kinase

Purification and partial characterization of cysteine-glutamate transaminase from rat liver

1977 ◽  
Vol 55 (9) ◽  
pp. 958-964 ◽  
Author(s):  
M. P. C. Ip ◽  
R. J. Thibert ◽  
D. E. Schmidt Jr.
Keyword(s):  
Molecular Weight ◽  
Rat Liver ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Liver Homogenate ◽  
Polyacrylamide Gel ◽  
Gel Chromatography ◽  
Labile Hydrogen ◽  
Apparent Homogeneity

Cysteine-glutamate transaminase (cysteine aminotransferase; EC 2.6.1.3) has been purified 149-fold to an apparent homogeneity giving a specific activity of 2.09 IU per milligram of protein with an overall yield of 15%. The isolation procedures involve the preliminary separation of a crude rat liver homogenate which was submitted sequentially to ammonium sulfate fractionation, TEAE-cellulose column chromatography, ultrafiltration, and isoelectrofocusing. The final product was homogenous when examined by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate (SDS). A minimal molecular weight of 83 500 was determined by Sephadex gel chromatography. The molecular weight as estimated by polyacrylamide gel electrophoresis in the presence of SDS was 84 000. The purified enzyme exhibited a pH optimum at 8.2 with cysteine and α-ketoglutarate as substrates. The enzyme is inactivated slowly when kept frozen and is completely inactivated if left at room temperature for 1 h. The enzyme does not catalyze the transamination of α-methyl-DL-cysteine, which, when present to a final concentration of 10 mM, exhibits a 23.2% inhibition of transamination of 30 mM of cysteine. The mechanism apparently resembles that of aspartate-glutamate transaminase (EC 2.6.1.1) in which the presence of a labile hydrogen on the alpha-carbon in the substrate is one of the strict requirements.

Studies of the metabolism of thiazolidine carboxylic acid by rat liver homogenate

1956 ◽  
Vol 22 (3) ◽  
pp. 558-564 ◽  
Author(s):  
D. Cavallini ◽  
C. De Marco ◽  
B. Mondovì ◽  
F. Trasarti
Keyword(s):  
Carboxylic Acid ◽  
Rat Liver ◽  
Liver Homogenate

Effect of adrenalectomy, sham operation or ACTH on the cortisol metabolizing enzymes of rat liver homogenate

Metabolism ◽  
1965 ◽  
Vol 14 (3) ◽  
pp. 264-270 ◽  
Author(s):  
R. Deckx ◽  
P. De Moor ◽  
C. Denef ◽  
J. Raus
Keyword(s):  
Rat Liver ◽  
Liver Homogenate ◽  
Sham Operation ◽  
Metabolizing Enzymes
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