Hydrolysis of exogenous ATP by isolated frog gastric mucosa.
ATP, added to the solution bathing the nutrient (serosal) surface of isolated frog gastric mucosa, was found to break down rapidly to ADP, inorganic phosphate and other products. This activity is due to an ectoenzyme, i.e. to an enzyme system easily accessible to the bathing solution. This conclusion follows from experiments which showed that penetration of ATP into the mucosal cells occurred at a much slower rate: leakage of inorganic phosphate and adenine nucleotides from mucosal cells was also minor. The surface ATPase may reflect the operation of a mechanism at the nutrient surface involved in acid secretion.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D001001:Anura; D003470:Culture Media; D005753:Gastric Mucosa / Q000378:metabolism*; D066298:In Vitro Techniques; D007700:Kinetics; D011892:Rana catesbeiana
D003470:Culture Media; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases