Enzymatic sulfation of gastrin in rat gastric mucosa
| Autor: | Lee J. Chen, Grace L. Rosenquist |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Phosphoadenosine Phosphosulfate
Biophysics Biochemistry Sulfation Gastrins Gastric mucosa medicine Animals Tyrosine Molecular Biology Gastrin chemistry.chemical_classification biology Adenine Nucleotides Chemistry Cell Biology Enzyme assay Rats medicine.anatomical_structure Enzyme Gastric Mucosa biology.protein Acid hydrolysis Sulfotransferases Arylsulfatase |
| Zdroj: | Biochemical and Biophysical Research Communications. 170:1170-1176 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/0006-291x(90)90516-p |
| Popis: | An enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to gastrin (G17) was identified in rat gastric mucosal cells. The enzyme activity was detected in the 105,000xg supernatant fraction. Formation of gastrin sulfate was shown by using 125I-gastrin and non-radioactive PAPS. The product was sensitive to acid hydrolysis, arylsulfatase treatment and removed by gastrin antibody, but not changed by treatments with chondro-4-sulfatase and chondro-6-sulfatase. The product had a molecular weight of 2050 daltons, close to the molecular weight of G17 sulfate, and, therefore, indicating the sulfated product is not APS derived from the degradation of PAPS. The enzyme activity showed a Km value of 5 microM for PAPS and a pH optimum of 6.0. The activity was not detected in the liver preparation. |
| Databáze: | OpenAIRE |
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