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CT chest showed a pattern of bilateral upper lobe mosaic attenuation and diffuse basilar predominant ground glass and peripheral reticular opacities with faint traction bronchiectasis suggesting non-specific interstitial pneumonia or possible hypersensitivity pneumonitis. There have been at least seven cases of drug-induced interstitial pneumonitis reported in the medical literature along with a smaller number of other venlafaxine associated pulmonary toxicities such as eosinophilic pneumonia and even asthma.

The binding of purified human erythrocyte AMP deaminase to human erythrocyte membranes and the effect of binding on enzyme catalytic activity was investigated. AMP deaminase binds preferentially and specifically to the cytoplasmic surface of the erythrocyte membrane. The binding is saturable, reversible, and responsive to alterations of pH, of ionic strength, and of ATP and AMP concentrations. A limited number (approximately equal to 2.2 X 10(4) per erythrocyte) of apparently homogeneous high affinity (Ka approximately equal to 2.6 X 10(7) M-1) binding sites is present. The stability of purified and endogenously bound AMP deaminase is markedly improved by the interaction with the membrane, whereas the catalytic activity of AMP deaminase is sharply reduced. AMP deaminase displaces membrane bound glyceraldehyde 3-phosphate dehydrogenase in roughly a dose-response manner. No evidence for binding of AMP deaminase to spectrin or band 3 (the G3PD binding protein) was found in sucrose gradients, however. The interaction of AMP deaminase with the erythrocyte membrane may play an important role in the regulation of cellular adenine nucleotide metabolism.The binding of purified human erythrocyte AMP deaminase to human erythrocyte membranes and the effect of binding on enzyme catalytic activity was investigated. AMP deaminase binds preferentially and specifically to the cytoplasmic surface of the erythrocyte membrane. The binding is saturable, reversible, and responsive to alterations of pH, of ionic strength, and of ATP and AMP concentrations. A limited number (approximately equal to 2.2 X 10(4) per erythrocyte) of apparently homogeneous high affinity (Ka approximately equal to 2.6 X 10(7) M-1) binding sites is present. The stability of purified and endogenously bound AMP deaminase is markedly improved by the interaction with the membrane, whereas the catalytic activity of AMP deaminase is sharply reduced. AMP deaminase displaces membrane bound glyceraldehyde 3-phosphate dehydrogenase in roughly a dose-response manner. No evidence for binding of AMP deaminase to spectrin or band 3 (the G3PD binding protein) was found in sucrose gradients, however. The interaction of AMP deaminase with the erythrocyte membrane may play an important role in the regulation of cellular adenine nucleotide metabolism.