Vasopressin is metabolized by a trypsinlike enzyme in guinea pig amniotic fluid
Autor: | A. K. Sato, C. F. T. Uyehara, J. R. Claybaugh |
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Rok vydání: | 1989 |
Předmět: |
endocrine system
Vasopressin medicine.medical_specialty Amniotic fluid Time Factors Physiology Vasopressins Endocrinology Diabetes and Metabolism Metabolite Trypsin inhibitor Guinea Pigs chemistry.chemical_compound Physiology (medical) Internal medicine medicine Animals Aprotinin Trypsin Chromatography High Pressure Liquid biology urogenital system Immune Sera Proteolytic enzymes Amniotic Fluid Endocrinology nervous system chemistry Enzyme inhibitor biology.protein Female hormones hormone substitutes and hormone antagonists medicine.drug |
Zdroj: | The American journal of physiology. 257(3 Pt 1) |
ISSN: | 0002-9513 |
Popis: | We have demonstrated that arginine vasopressin (AVP) is degraded to desglycinamide AVP by a trypsinlike enzyme found in guinea pig amniotic fluid. Incubation of [3H]AVP with guinea pig amniotic fluid in vivo or in vitro produced a metabolite that comigrated on high-pressure liquid chromatography with desglycinamide AVP in three different buffer systems. Also, AVP antisera that cross-reacted with standard desglycinamide AVP could detect this amniotic fluid metabolite. Because the enzyme responsible for the cleavage of glycinamide from AVP was likely to be trypsin, experiments with aprotinin, a trypsin inhibitor, were conducted. Results demonstrated that the production of the amniotic fluid AVP metabolite could be completely blocked in the presence of the trypsin inhibitor. In addition, examination of amniotic fluid collected from fetuses in the second half of gestation (term = 68 days) showed that AVP could not be metabolized to desglycinamide AVP until after 52 days of gestation. In conclusion, AVP appears to be metabolized by a trypsinlike enzyme in amniotic fluid, and because trypsin is a general proteolytic enzyme, the amniotic compartment may also serve as a clearance site for other proteins. |
Databáze: | OpenAIRE |
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