Structural information of butyrylcholinesterase (BChE) and its variants associated with
several diseases are discussed here. Pure human BChE has been proved safe and effective …

It is tacitly assumed that the biological role of acetylcholinesterase is termination of synaptic
transmission at cholinergic synapses. However, together with its structural homolog …

As a tetramer, acetylcholinesterase (AChE) is anchored to the basal lamina of the
neuromuscular junction and to the membrane of neuronal synapses. We have previously …

The atypical variant of human butyrylcholinesterase has Gly in place of Asp 70. Patients with
this D70G mutation respond abnormally to the muscle relaxant succinyldicholine …

The goal of this work was to determine what amino acids at the mouth of the active‐site
gorge are important for the function of human butyrylcholinesterase. Mutants D70G, Q119Y …

Human butyrylcholinesterase (BuChE) is a serine enzyme present in most organs and
plasma. No clear physiological function has yet been assigned to BuChE, but it is a …

Although aspirin (acetylsalicylic acid) is negatively charged, it is hydrolysed by
butyrylcholinesterase (BuChE). Catalytic parameters were determined in 100 mM Tris buffer …

The acetylcholine hydrolyzing enzyme, acetylcholinesterase, primarily functions in nerve
conduction, yet it appears in several guises, due to tissue-specific expression, alternative …

In vertebrates there are two cholinesterases, with differences in catalytic behaviour with
respect to substrate concentration: butyrylcholinesterase displays an increased activity at …

Butyrylcholinesterase from human plasma (HuBChE) is a potential drug candidate for
detoxification of certain harmful chemicals that contain carboxylic or phosphoric acid ester …