Comparative Studies on the Primary Structure of Acetylcholinesterases from Bovine Caudate Nucleus and Bovine Erythrocytes

Overview

Journal Cell Mol Neurobiol

Publisher Springer

Specialties Cell Biology
Molecular Biology
Neurology

Date 1991 Feb 1

PMID 2013055

Citations 1

Authors

H Heider

P Litynski

S Stieger

U Brodbeck

Affiliations

Soon will be listed here.

Abstract

1. Comparison of partial amino acid sequences of G2-acetylcholinesterase (AChE) from bovine erythrocytes and G4-AChE from bovine caudate nucleus revealed no differences in primary structure between the two enzymes. The first 33 residues of the N-terminal sequences were identical. 2. In addition, the amino acid sequences of four peptides generated by tryptic and cyanogen bromide cleavage were identical for bovine erythrocyte and brain AChE, suggesting one identical major coding exon for the adult bovine AChE forms. Comparison of these sequences with that of fetal bovine serum AChE (Doctor et al., 1988), showed differences in residues 16, 181, 212, and 216. 3. Deglycosylation studies of the two adult enzyme forms revealed that the core protein of erythrocyte AChE has an approximately 4 kDa lower molecular mass than brain AChE. This most probably reflects differences in the C-terminal sequences of the two enzymes.

Citing Articles

Monomerization of tetrameric bovine caudate nucleus acetylcholinesterase. Implications for hydrophobic assembly and membrane anchor attachment site.

Heider H, Brodbeck U Biochem J. 1992; 281 ( Pt 1):279-84.

PMID: 1731764 PMC: 1130674. DOI: 10.1042/bj2810279.

References

Sutton B, Phillips D . The three-dimensional structure of the carbohydrate within the Fc fragment of immunoglobulin G. Biochem Soc Trans. 1983; 11(2):130-2. View

Sorensen K, Gentinetta R, Brodbeck U . An amphiphile-dependent form of human brain caudate nucleus acetylcholinesterase: purification and properties. J Neurochem. 1982; 39(4):1050-60. DOI: 10.1111/j.1471-4159.1982.tb11496.x. View

Schumacher M, Camp S, Maulet Y, Newton M, Taylor S, Friedmann T . Primary structure of Torpedo californica acetylcholinesterase deduced from its cDNA sequence. Nature. 1986; 319(6052):407-9. DOI: 10.1038/319407a0. View

Bidlingmeyer B, Cohen S, Tarvin T . Rapid analysis of amino acids using pre-column derivatization. J Chromatogr. 1984; 336(1):93-104. DOI: 10.1016/s0378-4347(00)85133-6. View

Hall L, Spierer P . The Ace locus of Drosophila melanogaster: structural gene for acetylcholinesterase with an unusual 5' leader. EMBO J. 1986; 5(11):2949-54. PMC: 1167246. DOI: 10.1002/j.1460-2075.1986.tb04591.x. View

Grossmann H, LIEFLANDER M . [Acetylcholinesterase from bovine erythrocytes. Purification and properties of the enzyme solubilized in the presence and the absence of Triton X-100 (author's transl)]. Z Naturforsch C Biosci. 1979; 34(9-10):721-5. View

Sikorav J, Krejci E, Massoulie J . cDNA sequences of Torpedo marmorata acetylcholinesterase: primary structure of the precursor of a catalytic subunit; existence of multiple 5'-untranslated regions. EMBO J. 1987; 6(7):1865-73. PMC: 553570. DOI: 10.1002/j.1460-2075.1987.tb02445.x. View

Gennari K, Brunner J, Brodbeck U . Tetrameric detergent-soluble acetylcholinesterase from human caudate nucleus: subunit composition and number of active sites. J Neurochem. 1987; 49(1):12-8. DOI: 10.1111/j.1471-4159.1987.tb03386.x. View

Sikorav J, Duval N, Anselmet A, Bon S, Krejci E, Legay C . Complex alternative splicing of acetylcholinesterase transcripts in Torpedo electric organ; primary structure of the precursor of the glycolipid-anchored dimeric form. EMBO J. 1988; 7(10):2983-93. PMC: 454681. DOI: 10.1002/j.1460-2075.1988.tb03161.x. View

10.

Roberts W, Kim B, Rosenberry T . Differences in the glycolipid membrane anchors of bovine and human erythrocyte acetylcholinesterases. Proc Natl Acad Sci U S A. 1987; 84(22):7817-21. PMC: 299404. DOI: 10.1073/pnas.84.22.7817. View

11.

Chatonnet A, Lockridge O . Comparison of butyrylcholinesterase and acetylcholinesterase. Biochem J. 1989; 260(3):625-34. PMC: 1138724. DOI: 10.1042/bj2600625. View

12.

Bon S, Chang J, Strosberg A . Identical N-terminal peptide sequences of asymmetric forms and of low-salt-soluble and detergent-soluble amphiphilic dimers of Torpedo acetylcholinesterase. Comparison with bovine acetylcholinesterase. FEBS Lett. 1986; 209(2):206-12. DOI: 10.1016/0014-5793(86)81112-7. View

13.

Doctor B, Smyth K, Gentry M, Ashani Y, Christner C, de la Hoz D . Structural and immunochemical properties of fetal bovine serum acetylcholinesterase. Prog Clin Biol Res. 1989; 289:305-16. View

14.

Massoulie J, Bon S . The molecular forms of cholinesterase and acetylcholinesterase in vertebrates. Annu Rev Neurosci. 1982; 5:57-106. DOI: 10.1146/annurev.ne.05.030182.000421. View

15.

Laemmli U . Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227(5259):680-5. DOI: 10.1038/227680a0. View

16.

Tarentino A, Gomez C, PLUMMER Jr T . Deglycosylation of asparagine-linked glycans by peptide:N-glycosidase F. Biochemistry. 1985; 24(17):4665-71. DOI: 10.1021/bi00338a028. View

17.

Matsudaira P . Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J Biol Chem. 1987; 262(21):10035-8. View

18.

Rakonczay Z, Mallol J, Schenk H, Vincendon G, Zanetta J . Purification and properties of the membrane-bound acetylcholinesterase from adult rat brain. Biochim Biophys Acta. 1981; 657(1):243-56. DOI: 10.1016/0005-2744(81)90148-0. View

19.

Prody C, Zevin-Sonkin D, Gnatt A, Goldberg O, Soreq H . Isolation and characterization of full-length cDNA clones coding for cholinesterase from fetal human tissues. Proc Natl Acad Sci U S A. 1987; 84(11):3555-9. PMC: 304913. DOI: 10.1073/pnas.84.11.3555. View

20.

Doctor B, Chapman T, Christner C, Deal C, de la Hoz D, Gentry M . Complete amino acid sequence of fetal bovine serum acetylcholinesterase and its comparison in various regions with other cholinesterases. FEBS Lett. 1990; 266(1-2):123-7. DOI: 10.1016/0014-5793(90)81522-p. View