Ruthenium-Catalyzed Oxidative Dearomatization of N-Boc Indoles

Synthesis ◽  
2020 ◽  
Author(s):  
Xiao-Yu Zhou ◽  
Ming Bao ◽  
Xia Chen ◽  
Xiu-Juan Feng

AbstractRuthenium-catalyzed oxidative dearomatization of N-Boc indoles for the synthesis of indolin-3-ones is described. The N-Boc indoles can be transformed into indolin-3-ones in acetonitrile, using RuCl­3·3H2O as catalyst and sodium periodate (1.5 equiv) as oxidant. Further, a possible mechanism has been proposed on the basis of control experiments.

1988 ◽  
Vol 60 (02) ◽  
pp. 255-261 ◽  
Author(s):  
A Hotchkiss ◽  
C J Refino ◽  
C K Leonard ◽  
J V O'Connor ◽  
C Crowley ◽  
...  

SummaryModification of the carbohydrate structures of recombinant tissue-type plasminogen activator (rt-PA) can increase or decrease its rate of clearance in rabbits. When rt-PA was treated with sodium periodate to oxidize carbohydrate residues, the rate of clearance was decreased from 9.6 ± 1.9 ml min−1 kg−1 to 3.5 ± 0.6 ml min−1 kg−1 (mean ± SD, n = 5). A similar change in the clearance of rt-PA was introduced by the use of endo-β-N-acetyl- glucosaminidase H (Endo-H), which selectively removes high mannose asparagine-linked oligosaccharides; the clearance of Endo-H-treated rt-PA was 5.0 ± 0.5 ml min−1 kg−1. A mutant of rt-PA was produced with an amino acid substitution at position 117 (Asn replaced with Gin) to remove a potential glycosylation site that normally contains a high mannose structure. The clearance of this material was also decreased, similar to the periodate and Endo-H-treated rt-PA. Conversely, when rt-PA was produced in the CHO 15B cell line, which can produce only high mannose oligosaccharide structures on glycoproteins, the clearance was increased by a factor of 1.8. These results demonstrate that the removal of rt-PA from the blood depends significantly upon the nature of its oligosaccharide structures.


2011 ◽  
Vol 3 (5) ◽  
pp. 585-588
Author(s):  
B Dharma Rao B Dharma Rao ◽  
◽  
M Sridevi M Sridevi ◽  
P Vani P Vani

1975 ◽  
Vol 74 (1) ◽  
pp. 35-41 ◽  
Author(s):  
M. R. Hollingdale

SUMMARYA serological analysis of mycelial antigens ofThermoactinomyces vulgarisin immunodiffusion with human sera revealed five individual antigens. Three antigens were proteins, sensitive to pronase and soluble in phenol. Two were cationic polysaccharides, sensitive to sodium periodate, and containing glucosamine and muramic acid.Latex coated with mycelial antigens was compared with precipitin tests in detecting antibodies toT. vulgaris;the number of positive results detected by each test differed slightly, and a combination of the two tests detected the highest number. Counterimmunoelectrophoresis (CIE) was shown to be a very sensitive method for detecting precipitins, but not for their measurement. A prospective evaluation of immunodiffusion, latex agglutination and CIE as potential serodiagnostic techniques for farmer's lung disease is suggested.


2005 ◽  
Vol 242 (1-2) ◽  
pp. 251-255 ◽  
Author(s):  
Valiollah Mirkhani ◽  
Shahram Tangestaninejad ◽  
Majid Moghadam ◽  
Iraj Mohammadpoor-Baltork ◽  
Hadi Kargar

2006 ◽  
Vol 45 (44) ◽  
pp. 7433-7436 ◽  
Author(s):  
Takao Osako ◽  
Eric J. Watson ◽  
Ahmad Dehestani ◽  
Brian C. Bales ◽  
James M. Mayer

2002 ◽  
Vol 43 (48) ◽  
pp. 8727-8729 ◽  
Author(s):  
Mijuan Wang ◽  
Chun Li ◽  
Dali Yin ◽  
Xiao-Tian Liang

2011 ◽  
Vol 175-176 ◽  
pp. 214-219 ◽  
Author(s):  
Yun Hui Xu ◽  
Zhao Fang Du ◽  
Yu Yue Chen

For exploiting the novel multifunctional ecological cotton fibers, a new cotton fiber with the collagen protein cross-linking (CPCCF) was prepared by the limited selective oxidation of a cotton thread with sodium periodate solution and subsequent treatment with a solution of collagen protein at 40°C in aqueous acetic acid. FT-IR spectra of the CPCCF suggested that the imine covalent bond between the collagen protein and the oxidized cotton fiber was formed through a series of reaction. X-ray diffractograms analysis showed that the crystallinity of oxidized cotton fiber after collagen protein treatment increased slightly. Meanwhile, Scanning electron microscopy photographs illuminated that the modification with collagen protein occurred on the surface of cotton fiber. Kjeldahl nitrogen analysis of the CPCCF showed that the maximum percentage of collagen protein introduced into cotton fiber was 1.68% (w/w). However, the breaking strength of the cotton thread oxidized partially by sodium periodate at the concentration of less than 2.0 mg ml-1 did not decrease much. Furthermore, a model experiment for the controlled release drugs was performed using aloe anthraquinone, components of a Chinese medicine, suggested potential usefulness of the CPCCF as a carrier for the controlled release drugs.


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