ISSN:
1573-6830
Keywords:
acetylcholinesterase
;
amino acid sequence
;
amino acid analysis
;
bovine brain
;
bovine erythrocytes
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Summary 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 enyzmes. 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 erthyrocyte 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 (Doctoret 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 propably reflects differences in the C-terminal sequences of the two enzymes.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00712803
Permalink