1989
DOI: 10.1016/s0021-9258(18)83774-7
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Proteolytic modification of Escherichia coli alkaline phosphatase

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1989
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Cited by 14 publications
(4 citation statements)
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“…However, it appears more likely that Mg 2+ binding causes long-range intersubunit interactions that change the overall AP structure significantly. This agrees with previous results from experiments with trypsin-modified AP hybrid dimers which revealed that the modified subunit altered the structural and kinetic properties of the other subunit through subunit interactions ( ). NMR studies of metal hybrid AP dimers, with Zn 2+ bound to one subunit and Cd 2+ bound to the other, have found that Zn 2+ binding caused substantial changes in the chemical shift of the Cd 2+ ligands over 30 Å away at the other active site, again demonstrating long distance subunit interactions ().…”
Section: Discussionsupporting
confidence: 92%
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“…However, it appears more likely that Mg 2+ binding causes long-range intersubunit interactions that change the overall AP structure significantly. This agrees with previous results from experiments with trypsin-modified AP hybrid dimers which revealed that the modified subunit altered the structural and kinetic properties of the other subunit through subunit interactions ( ). NMR studies of metal hybrid AP dimers, with Zn 2+ bound to one subunit and Cd 2+ bound to the other, have found that Zn 2+ binding caused substantial changes in the chemical shift of the Cd 2+ ligands over 30 Å away at the other active site, again demonstrating long distance subunit interactions ().…”
Section: Discussionsupporting
confidence: 92%
“…The B sites bind Zn 2+ more strongly in the presence of phosphate and can also bind Mg 2+ at high concentrations (14); however, Mg 2+ normally occupies the C sites. There appears to be significant cooperativity among metal binding sites and between the two subunits (15,(17)(18)(19)(20)(21).…”
mentioning
confidence: 99%
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“…The enzymatic activities of AP and the scFv-AP fusion protein were measured according to the method described by Tyler-Cross et al 26 The kinetics parameters were determined on the basis of utilizing p-NPP as the substrate. One unit of enzyme was dened as the quantity required for liberating 1 mM of 4-nitrophenol per h. 27 The reaction was monitored at 25 C by following the increase in absorbance at 405 nm (A405 nm) in a 1 M Tris-HCl buffer (pH ¼ 8.0) containing 10 mM MgCl 2 and 50 mM ZnCl 2 .…”
Section: Enzymatic Activity Analysismentioning
confidence: 99%