engleski

SELECTIVE-INHIBITION OF ALKALINE-PHOSPHATASES - LIMITED ACCESS OF THE ESCHERICHIA-COLI ACTIVE- SITE TO DIALKYL SUBSTITUTED PHENYL PHOSPHATES

The structural interrelationship and catalytic specifities of E. coli, calf intestinal and human alkaline phosphatases were investigated. The inhibition studies were performed using a variety of structural related alternative substrates i.e. dialkyl substituted phenyl phosphates. The absence of a major steric effect for disubstituted aryl monophosphates indicates considerable freedom of the leaving group in the ES complex of human ALPs. Calf intestinal and E. coli ALP behave in a similar manner being much less affected by the different inhibitors. The steric specifity of E. coli ALP is evidenced by the findings that bulky ortho-substituents on the aryl function reduce the inhibitory response of the respective alternative substrates.

Isoenzymes ; Liver, CDNA ; Bone

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