An improvement in segregation of human butyrylcholinesterase phenotypes having the fluoride-resistant variants.

نویسندگان

  • Zrinka Kovarik
  • Vera Simeon-Rudolf
چکیده

Correct recognition of butyrylcholinesterase (BChE; EC 3.1.1.8) variants in human serum is essential if patients susceptible to a prolonged reaction following treatment with short acting muscle relaxants, like suxamethonium, are to be reliably identified. The dimethylcarbamate Ro 02-0683 is used in standard procedures for identification of BChE variant by measuring residual activity after two hours of inhibition. Such a long inhibition time distinguishes well between the usual (U) and atypical (A), but less successfully the fluoride-resistant (F) variant. In this paper, inhibition rate constants were determined from the initial time course of inhibition of homozygous (FF) and heterozygous (UF and AF) BChE phenotypes by Ro 02-0683; 1.6 x 10(6), 2.7 x 10(6) and 6.2 x 10(6) dm3 mol-1 min-1 for AF, FF and UF, respectively. After only 30 min of inhibition the resolution between the phenotypes was even better than after two hours. Hence, determination of the residual activity after 30 min inhibition is recommended for the segregation of the suxamethonium sensitive fluoride-resistant variants.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

The effect of temperature on fluoride-resistant serum cholinesterase.

By means of dibucaine inhibition (Kalow and Genest, 1957) it was found possible to differentiate three inherited serum cholinesterase phenotypes, those homozygous for the usual enzyme, homozygotes of the atypical enzyme and heterozygous individuals (Kalow and Staron, 1957). Harris and Whittaker (1961) then showed that sodium fluoride could be used to differentiate the serum cholinesterase varia...

متن کامل

Genotyping the butyrylcholinesterase in patients with prolonged neuromuscular block after succinylcholine.

BACKGROUND Succinylcholine remains the standard neuromuscular blocking drug for tracheal intubation in emergency situations. The short duration of action is due to its rapid hydrolytic degradation by butyrylcholinesterase (plasmacholinesterase). Multiple variants of this enzyme are known (A, F, S, H, J, K variants) with different effects on enzyme activity. This study was undertaken to evaluate...

متن کامل

Identification of human butyrylcholinesterase organophosphate-resistant variants through a novel mammalian enzyme functional screen.

Human butyrylcholinesterase (hBChE) is currently being developed as a detoxication enzyme for the catalytic hydrolysis or stoichiometric binding of organophosphates (OPs). Previously, rationally designed hBChE mutants (G117H and E197Q) were reported in the literature and showed the feasibility of engineering OP hydrolytic functional activity into hBChE. However, the OP hydrolysis rate for G117H...

متن کامل

Recombinant human butyrylcholinesterase G390V, the fluoride-2 variant, expressed in Chinese hamster ovary cells, is a low affinity variant.

Kinetics of recombinant fluoride-2 variant of human butyrylcholinesterase (Gly390 Val) secreted by Chinese hamster ovary cells were compared to recombinant usual and to usual butyrylcholinesterase purified from human plasma. The usual and fluoride-2 variant were indistinguishable with regard to hydrolysis of benzoylcholine (Km = 5 microM), neutral esters, and at high concentrations of acetylthi...

متن کامل

Butyrylcholinesterase Genetic Variants: Association with Cocaine Dependence and Related Phenotypes

OBJECTIVE The search for genetic vulnerability factors in cocaine dependence has focused on the role that neuroplasticity plays in addiction. However, like many other drugs, the ability of an individual to metabolize cocaine can also influence susceptibility to dependence. Butyrylcholinesterase (BChE) metabolizes cocaine, and genetic variants of the BChE gene (BCHE) alter its catalytic activity...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Arhiv za higijenu rada i toksikologiju

دوره 54 4  شماره 

صفحات  -

تاریخ انتشار 2003