Thionaphthylation of Active Site of Heavy Meromyosin Adenosine Triphosphatase by Disulfide Exchange Reaction*

1969 ◽  
Vol 66 (6) ◽  
pp. 751-758
Author(s):  
MASAHIKO ONODERA ◽  
KOICHI YAGI
Keyword(s):  
Exchange Reaction ◽  
Active Site ◽  
Adenosine Triphosphatase ◽  
Heavy Meromyosin ◽  
Disulfide Exchange

Pyridyl disulfide-based thiol–disulfide exchange reaction: shaping the design of redox-responsive polymeric materials

2020 ◽  
Vol 11 (48) ◽  
pp. 7603-7624
Author(s):  
Ismail Altinbasak ◽  
Mehmet Arslan ◽  
Rana Sanyal ◽  
Amitav Sanyal
Keyword(s):  
Exchange Reaction ◽  
Functional Materials ◽  
Polymeric Materials ◽  
Disulfide Exchange ◽  
Redox Responsive ◽  
Synthetic Approaches

This review provides an overview of synthetic approaches utilized to incorporate the thiol-reactive pyridyl-disulfide motif into various polymeric materials, and briefly highlights its utilization to obtain functional materials.

scholarly journals On the Active Site of Myosin A-Adenosine Triphosphatase

1961 ◽  
Vol 236 (7) ◽  
pp. 1968-1972 ◽  
Author(s):  
Yuji Tonomura ◽  
Junko Yoshimura ◽  
Shotaro Kitagawa
Keyword(s):  
Active Site ◽  
Adenosine Triphosphatase

Poly(ε-caprolactone) with pendant natural peptides: an old polymeric biomaterial with new properties

2017 ◽  
Vol 8 (35) ◽  
pp. 5415-5426 ◽  
Author(s):  
Yuanyuan Ju ◽  
Mingming Zhang ◽  
Hanying Zhao
Keyword(s):  
Click Chemistry ◽  
Exchange Reaction ◽  
Ring Opening ◽  
The Self ◽  
Disulfide Exchange ◽  
Polymeric Biomaterial ◽  
Natural Peptides

Poly(ε-caprolactone) with pendant glutathione or l-carnosine was synthesized by a combination of ring-opening copolymerization, click chemistry and thiol-disulfide exchange reaction, and the self-assemblies of the polymers were investigated.

Thiol derivatives of cellulose as supports for the immobilization of non-thiol enzymes

1981 ◽  
Vol 46 (7) ◽  
pp. 1693-1700 ◽  
Author(s):  
Peter Gemeiner ◽  
Jiří Zemek
Keyword(s):  
Exchange Reaction ◽  
Proteolytic Activity ◽  
Acetylcholine Esterase ◽  
Mercaptoacetic Acid ◽  
Thiol Groups ◽  
Nucleophilic Reaction ◽  
Disulfide Exchange ◽  
Immobilized Trypsin ◽  
Esterolytic Activity ◽  
Derivatives Of

Thiosulfate derivatives, which can be reduced with mercaptoacetic acid, are suitable intermediates for the preparation of thiol derivatives of polymers. Thiosulfate derivatives of cellulose were prepared via chlorodeoxy- or via 3-chloro-2-hydroxy-propylcellulose, while mercaptodeoxycellulose prepared via chlorodeoxy derivative had more convenient properties for the immobilization of non-thiol enzymes (acetylcholine esterase, butyrylcholine esterase and trypsin). Before immobilization SH groups were introduced into choline esterases by i) reduction of the cystine residues, ii) reaction with methyl 4-mercaptobutyrimidate, and the isothiocyanate groups were introduced into trypsin on reaction with 3-isothiocyanatopropyl 1-isocyanate. The immobilization of the enzymes treated in this way was carried out under the conditions of the oxidation of thiol groups (i), thiol-disulfide exchange reaction (ii), or an addition nucleophilic reaction of isothiocyanates with thiols. In contrast to the proteolytic activity of the immobilized trypsin the esterolytic activity of immobilized choline esterases attained satisfactory values.

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