These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • Title: Primary structure of peptides from bovine brain glutamine synthetase. Comparison with sequences of glutamine synthetases from other organisms.
    Author: Johnson RJ, Piskiewicz D.
    Journal: Biochim Biophys Acta; 1985 Mar 01; 827(3):439-46. PubMed ID: 2857576.
    Abstract:
    An analysis of the covalent structure of bovine brain glutamine synthetase has been initiated. Cyanogen bromide and tryptic digests have yielded peptides accounting for most of the polypeptide subunit, and sequence analysis has placed in order over half of the amino acids within these peptides. The amino terminus is acetylated and has the following partial sequence: Ac(H, S3, A2, T)-L-B-K-G-I-K-Z-V-Y-M. The carboxyl-terminal sequence is: A-L-P-Q-G-D-K-V-Q-A-M. The peptides isolated from bovine glutamine synthetase show a high degree of homology with peptides isolated from ovine and porcine brain glutamine synthetases. In contrast to the sequence homologies of the proteins from eukaryotic sources, there are no obvious amino acid sequence homologies between bovine brain glutamine synthetase and any prokaryotic glutamine synthetase. Bovine brain glutamine synthetase is inactivated by phenylglyoxal and N-ethylmaleimide. In both cases catalytic activity is protected by the presence of ATP, suggesting the presence of arginine and cysteine residues at or near the ATP binding site.
    [Abstract] [Full Text] [Related] [New Search]