Deaminative Reductive Methylation of Alkylpyridinium Salts

2021 ◽  
Vol 23 (18) ◽  
pp. 7059-7063
Author(s):  
Olivia P. Bercher ◽  
Shane Plunkett ◽  
Thomas E. Mortimer ◽  
Mary P. Watson
Keyword(s):  
Reductive Methylation

scholarly journals Characterization of [3H]palmitate- and [3H]ethanolamine-labelled proteins in the multicellular parasitic trematode Schistosoma mansoni

1988 ◽  
Vol 254 (2) ◽  
pp. 419-426 ◽  
Author(s):  
P M Wiest ◽  
E J Tisdale ◽  
W L Roberts ◽  
T L Rosenberry ◽  
A A F Mahmoud ◽  
...  
Keyword(s):  
Schistosoma Mansoni ◽  
Molecular Mass ◽  
Gel Electrophoresis ◽  
Free Amino ◽  
Protein Modification ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Reductive Methylation ◽  
Amide Linkage

Biosynthetic labelling experiments with cercariae and schistosomula of the multicellular parasitic trematode Schistosoma mansoni were performed to determine whether [3H]palmitate or [3H]ethanolamine was incorporated into proteins. Parasites incorporated [3H]palmitate into numerous proteins, as judged by SDS/polyacrylamide-gel electrophoresis and fluorography. The radiolabel was resistant to extraction with chloroform, but sensitive to alkaline hydrolysis, indicating the presence of an ester bond. Further investigation of the major 22 kDa [3H]palmitate-labelled species showed that the label could be recovered in a Pronase fragment which bound detergent and had an apparent molecular mass of 1200 Da as determined by gel filtration on Sephadex LH-20. Schistosomula incubated with [3H]ethanolamine for up to 24 h incorporated this precursor into several proteins; labelled Pronase fragments recovered from the three most intensely labelled proteins were hydrophilic and had a molecular mass of approx. 200 Da. Furthermore, reductive methylation of such fragments showed that the [3H]ethanolamine bears a free amino group, indicating the lack of an amide linkage. We also evaluated the effect of phosphatidylinositol-specific phospholipase C from Staphylococcus aureus: [3H]palmitate-labelled proteins of schistosomula and surface-iodinated proteins were resistant to hydrolysis with this enzyme. In conclusion, [3H]palmitate and [3H]ethanolamine are incorporated into distinct proteins of cercariae and schistosomula which do not bear glycophospholipid anchors. The [3H]ethanolamine-labelled proteins represent a novel variety of protein modification.

scholarly journals Chemistry of bleomycin. XXV. Reductive methylation of bleomycin, a chemical proof for the presence of the free secondary amine in bleomycin.

1980 ◽  
Vol 33 (1) ◽  
pp. 114-117 ◽  
Author(s):  
TAKEYD FUKUOKA ◽  
YASUHIKO MURAOKA ◽  
AKIO FUJII ◽  
HIROSHI NAGANAWA ◽  
TOMOHISA TAKITA ◽  
...  
Keyword(s):  
Secondary Amine ◽  
Reductive Methylation

Copper(II)-Catalyzed Selective Reductive Methylation of Amines with Formic Acid: An Option for Indirect Utilization of CO2

2017 ◽  
Vol 19 (6) ◽  
pp. 1490-1493 ◽  
Author(s):  
Chang Qiao ◽  
Xiao-Fang Liu ◽  
Xi Liu ◽  
Liang-Nian He
Keyword(s):  
Formic Acid ◽  
Reductive Methylation

Safe and Efficient Reductive Methylation of Primary and Secondary Amines UsingN-Methylpyrrolidine Zinc Borohydride

2010 ◽  
Vol 40 (16) ◽  
pp. 2415-2420 ◽  
Author(s):  
Heshmatollah Alinezhad ◽  
Mahmood Tajbakhsh ◽  
Fatemeh Salehian ◽  
Kazem Fazli
Keyword(s):  
Secondary Amines ◽  
Reductive Methylation ◽  
Primary And Secondary Amines

In vitro labeling of proteins by reductive methylation: Application to proteins involved in supramolecular structures

1982 ◽  
Vol 19 (1) ◽  
pp. 77-91 ◽  
Author(s):  
C. S. Heacock ◽  
B. W. Bernstein ◽  
A. S. Duhaiman ◽  
D. A. Amorese ◽  
J. R. Bamburg
Keyword(s):  
Supramolecular Structures ◽  
Reductive Methylation

scholarly journals Large-scale evaluation of protein reductive methylation for improving protein crystallization

2008 ◽  
Vol 5 (10) ◽  
pp. 853-854 ◽  
Author(s):  
Youngchang Kim ◽  
Pearl Quartey ◽  
Hui Li ◽  
Lour Volkart ◽  
Catherine Hatzos ◽  
...  
Keyword(s):  
Large Scale ◽  
Protein Crystallization ◽  
Reductive Methylation ◽  
Scale Evaluation
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