| Autor: |
Yao, Rong, Nimec, Zenia, Ryan, Thomas J., Galivan, John |
| Zdroj: |
Journal of Biological Chemistry; April 1996, Vol. 271 Issue: 15 p8525-8528, 4p |
| Abstrakt: |
Purified -glutamyl hydrolase secreted from rat H35 hepatoma cells has been characterized as a diffuse band of 55 kDa on SDS-polyacrylamide gel electrophoresis that is converted to bands of 35 and 33 kDa after enzymatic removal of N-linked carbohydrate. Polyclonal antibodies against 55-kDa -glutamyl hydrolase captured the enzyme activity and recognized the glycosylated and both deglycosylated forms of -glutamyl hydrolase. A complete cDNA sequence of -glutamyl hydrolase was obtained using degenerate oligonucleotides derived from peptide sequences, screening of a rat hepatoma cDNA library, and reverse transcription polymerase chain reaction. Based upon the deduced amino acid sequence the peptide component of -glutamyl hydrolase had a molecular weight of 33,400. The results of amino acid analysis of the purified protein agreed with the deduced amino acid sequence in which there are seven potential asparagine-containing glycosylation sites. |
| Databáze: |
Supplemental Index |
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