TY - JOUR
T1 - Determination of the DNA sequences of acetylcholinesterase and butyrylcholinesterase from cat and demonstration of the existence of both in cat plasma
AU - Bartels, Cynthia F.
AU - Xie, Weihua
AU - Miller-Lindholm, Amanda K.
AU - Schopfer, Lawrence M.
AU - Lockridge, Oksana
N1 - Funding Information:
Dr. Naida Lustakoff and Dr. Doug Armstrong of the Henry Doorly Zoo, Omaha, provided Bengal tiger blood and pituitary gland. The UNMC Comparative Medicine Department provided pooled cat blood and cat pituitary gland. Stacy Wieseler, supported by the Minority Student and Sciences Teacher Training Program, National Center for Research Resources, Grant R25RR10280, helped to purify cat BChE. The UNMC Molecular Biology Core Facility provided oligonucleotide primers and DNA sequencing. The UNMC Molecular Modeling Core Facility provided protein models of BChE, and technical support. Both facilities were supported, in part, by Cancer Center Support Grant P30 CA36727 to the Eppley Institute. This work was supported by US Army Medical Research and Development Command Grants DAMD17–94-J-4005 and DAMD17–97-1–7349 (to O. L.) The opinions or assertions contained herein belong to the authors and should not be construed as the official views of the U.S. Army or the Department of Defense.
PY - 2000/8/15
Y1 - 2000/8/15
N2 - Cat serum contains 0.5 mg/L of butyrylcholinesterase (BChE, EC 3.1.1.8) and 0.3 mg/L of acetylcholinesterase (AChE, EC 3.1.1.7); this can be compared with 5 mg/mL and < 0.01 mg/L, respectively, in human serum. Cat BChE differed from human BChE in the steady-state turnover of butyrylthiocholine, having a 3-fold higher k(cat) and 2-fold higher K(m) and K(ss) values. Sequencing of the cat BCHE cDNA revealed 70 amino acid differences between cat and human BChE, three of which could account for these kinetic differences. These amino acids, which were located in the region of the active site, were Phe398Ile, Pro285Leu, and Ala277Leu (where the first amino acid was found in human and the second in cat). Sequencing genomic DNA for cat and human ACHE demonstrated that there were 33 amino acid differences between the cat and human AChE enzymes, but that there were no differences in the active site region. In addition, a polymorphism in intron 3 of the human ACHE gene was detected, as well as a silent polymorphism at Y116 of the cat ACHE gene. Copyright (C) 2000 Elsevier Science Inc.
AB - Cat serum contains 0.5 mg/L of butyrylcholinesterase (BChE, EC 3.1.1.8) and 0.3 mg/L of acetylcholinesterase (AChE, EC 3.1.1.7); this can be compared with 5 mg/mL and < 0.01 mg/L, respectively, in human serum. Cat BChE differed from human BChE in the steady-state turnover of butyrylthiocholine, having a 3-fold higher k(cat) and 2-fold higher K(m) and K(ss) values. Sequencing of the cat BCHE cDNA revealed 70 amino acid differences between cat and human BChE, three of which could account for these kinetic differences. These amino acids, which were located in the region of the active site, were Phe398Ile, Pro285Leu, and Ala277Leu (where the first amino acid was found in human and the second in cat). Sequencing genomic DNA for cat and human ACHE demonstrated that there were 33 amino acid differences between the cat and human AChE enzymes, but that there were no differences in the active site region. In addition, a polymorphism in intron 3 of the human ACHE gene was detected, as well as a silent polymorphism at Y116 of the cat ACHE gene. Copyright (C) 2000 Elsevier Science Inc.
KW - Acetylcholinesterase
KW - Cholinesterase
KW - Feline
KW - Felis
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U2 - 10.1016/S0006-2952(00)00365-8
DO - 10.1016/S0006-2952(00)00365-8
M3 - Article
C2 - 10874122
AN - SCOPUS:0034664228
SN - 0006-2952
VL - 60
SP - 479
EP - 487
JO - Biochemical Pharmacology
JF - Biochemical Pharmacology
IS - 4
ER -