Cloning of cDNA coding for guinea pig liver transglutaminase.

1 January 1987

journal article
Published by Oxford University Press (OUP) in Agricultural and Biological Chemistry

Vol. 51 (3) , 957-961
https://doi.org/10.1271/bbb1961.51.957

Abstract

Seven peptides derived from guinea pig liver transglutaminase were sequenced. Using synthetic oligonucleotides that we designed from the amino acid sequences as probes, we obtained a cDNA clone of transglutaminase from a cDNA library constructed with mRNA partly purified from guinea pig liver. About 60% of the primary structure of enzyme protein was predicted by sequencing of the cDNA. The predicted amino acid sequence included a sequence of pentapeptide containing the active-site cysteine residue [J. E. Folk and P. W. Cole, J. Biol. Chem., 241, 3238 (1966)]. An expanded region of the sequence surrounding the active-site cysteine residue showed significant homology to that of thiol proteases. Two regions rich in glutamic acid residues were found; they are possible calcium-binding sites of this enzyme.

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