Trp82 and Tyr332 Are Involved in Two Quaternary Ammonium Binding Domains of Human Butyrylcholinesterase as Revealed by Photoaffinity Labeling with [3H]DDF†

Biochemistry ◽  
1998 ◽  
Vol 37 (29) ◽  
pp. 10507-10513 ◽  
Author(s):  
Florian Nachon ◽  
Laurence Ehret-Sabatier ◽  
Damarys Loew ◽  
Christophe Colas ◽  
Alain van Dorsselaer ◽  
...  
Keyword(s):  
Quaternary Ammonium ◽  
Photoaffinity Labeling ◽  
Binding Domains ◽  
Ammonium Binding ◽  
Human Butyrylcholinesterase

The Uptake of Picloram by Potato Tuber Tissue

Weed Science ◽  
1970 ◽  
Vol 18 (1) ◽  
pp. 22-24 ◽  
Author(s):  
J. R. Baur ◽  
R. W. Bovey
Keyword(s):  
Solanum Tuberosum ◽  
Potato Tuber ◽  
Quaternary Ammonium ◽  
Binding Sites ◽  
Cetyl Trimethyl Ammonium Bromide ◽  
Ammonium Bromide ◽  
Potato Tissue ◽  
Tuber Tissue ◽  
Cetyl Trimethyl Ammonium ◽  
Ammonium Binding

Pretreatment of potato (Solanum tuberosumL., var. Russet) tuber discs in pH 5.5 buffer significantly reduced uptake of picloram (10−3M). Tissue pretreated in buffer at 7 C subsequently absorbed more picloram than tissue pretreated at 25 C. Inclusion of cetyl trimethyl ammonium bromide (hereinafter referred to as CTAB) (2 × 10−4M) in the treating solution caused a significant increase in picloram uptake in tissues that were not pretreated in buffer. The reduction in uptake caused by buffer pretreatment was effectively reversed when CTAB was included in the treating solution. The results suggest that picloram uptake by potato tissue is related to the availability of the quaternary ammonium binding sites provided by membrane phosphatides.

Delineation and Decomposition of Energies Involved in Quaternary Ammonium Binding in the Active Site of Acetylcholinesterase

2000 ◽  
Vol 122 (13) ◽  
pp. 2975-2980 ◽  
Author(s):  
Daniel M. Quinn ◽  
Shawn R. Feaster ◽  
Haridasan K. Nair ◽  
Nathan A. Baker ◽  
Zoran Radić ◽  
...  
Keyword(s):  
Active Site ◽  
Quaternary Ammonium ◽  
Ammonium Binding

scholarly journals Identification of Peptide Ligand-binding Domains within the Human Motilin Receptor Using Photoaffinity Labeling

2001 ◽  
Vol 276 (38) ◽  
pp. 35518-35522 ◽  
Author(s):  
Bernard Coulie ◽  
Bunzo Matsuura ◽  
Maoqing Dong ◽  
Elizabeth M. Hadac ◽  
Delia I. Pinon ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Photoaffinity Labeling ◽  
Peptide Ligand ◽  
Binding Domains ◽  
Motilin Receptor

Catalyst- and oxidant-free electrochemical para-selective hydroxylation of N-arylamides in batch and continuous-flow

2020 ◽  
Vol 22 (19) ◽  
pp. 6437-6443
Author(s):  
Cheng-Kou Liu ◽  
Meng-Yi Chen ◽  
Xin-Xin Lin ◽  
Zheng Fang ◽  
Kai Guo
Keyword(s):  
Ammonium Salt ◽  
Quaternary Ammonium ◽  
Continuous Flow ◽  
Quaternary Ammonium Salt ◽  
Selective Hydroxylation

A catalyst-, oxidant-, acidic solvent- and quaternary ammonium salt-free electrochemical para-selective hydroxylation of N-arylamides at rt in batch and continuous-flow was developed.

Genomic analysis of C-type lectins

2002 ◽  
Vol 69 ◽  
pp. 59-72 ◽  
Author(s):  
Kurt Drickamer ◽  
Andrew J. Fadden
Keyword(s):  
Biological Effects ◽  
Cell Signalling ◽  
Genomic Analysis ◽  
Binding Activity ◽  
Immunoglobulin Superfamily ◽  
Carbohydrate Binding ◽  
Carbohydrate Recognition ◽  
Calcium Dependent ◽  
Binding Domains ◽  
Carbohydrate Recognition Domains

Many biological effects of complex carbohydrates are mediated by lectins that contain discrete carbohydrate-recognition domains. At least seven structurally distinct families of carbohydrate-recognition domains are found in lectins that are involved in intracellular trafficking, cell adhesion, cell–cell signalling, glycoprotein turnover and innate immunity. Genome-wide analysis of potential carbohydrate-binding domains is now possible. Two classes of intracellular lectins involved in glycoprotein trafficking are present in yeast, model invertebrates and vertebrates, and two other classes are present in vertebrates only. At the cell surface, calcium-dependent (C-type) lectins and galectins are found in model invertebrates and vertebrates, but not in yeast; immunoglobulin superfamily (I-type) lectins are only found in vertebrates. The evolutionary appearance of different classes of sugar-binding protein modules parallels a development towards more complex oligosaccharides that provide increased opportunities for specific recognition phenomena. An overall picture of the lectins present in humans can now be proposed. Based on our knowledge of the structures of several of the C-type carbohydrate-recognition domains, it is possible to suggest ligand-binding activity that may be associated with novel C-type lectin-like domains identified in a systematic screen of the human genome. Further analysis of the sequences of proteins containing these domains can be used as a basis for proposing potential biological functions.

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