Evidence for Tissue-Specific Forms of Glutaminyl Cyclase

Authors

Paul A. Sykes, University of Southern Mississippi
Stephanie J. Watson, University of Southern Mississippi
Jeffrey S. Temple, University of Southern Mississippi
Robert C. Bateman Jr., University of Southern MississippiFollow

Document Type

Article

Publication Date

7-16-1999

Department

Chemistry and Biochemistry

School

Mathematics and Natural Sciences

Abstract

Glutaminyl cyclase (QC) is responsible for the presence of pyroglutamyl residues in many neuroendocrine peptides, An examination of the bovine tissue distribution of QC immunoreactivity, enzyme activity, and mRNA confirmed that QC was abundant in brain and pituitary by all three measures. However, enzymatic activity was considerably more widespread than either immunoreactivity or mRNA, suggesting multiple enzyme forms. Partially purified QC from bovine spleen differed significantly from the known bovine pituitary QC in physical and catalytic properties. We propose that this form of glutaminyl cyclase plays a role in the posttranslational processing of constitutively secreted pGlu-containing proteins, (C) 1999 Federation of European Biochemical Societies.

Publication Title

FEBS Letters

Volume

455

Issue

41276

First Page

159

Last Page

161

Recommended Citation

Sykes, P. A., Watson, S. J., Temple, J. S., Bateman, R. C. (1999). Evidence for Tissue-Specific Forms of Glutaminyl Cyclase. FEBS Letters, 455(41276), 159-161.
Available at: https://aquila.usm.edu/fac_pubs/9236