65Zn(II), 115mCd(II), 60Co(II), and mg(II) binding to alkaline phosphatase of Escherichia coli. Structural and functional effects.

Functional and structural properties of immobilized subunits of Escherichia coli alkaline phosphatase.

Alkaline phosphatase from Escherichia coli has been immobilized on Sepharose CL-4B using low levels of cyanogen bromide activation in order to favor the attachment of the dimer to the support through a single covalent linkage. The matrix-bound subunits obtained after dissociation of the immobilized dimer were shown to be catalytically inactive by three different criteria: 1) The level of phosph...

Functional interrelationships in the alkaline phosphatase superfamily: phosphodiesterase activity of Escherichia coli alkaline phosphatase.

Escherichia coli alkaline phosphatase (AP) is a proficient phosphomonoesterase with two Zn(2+) ions in its active site. Sequence homology suggests a distant evolutionary relationship between AP and alkaline phosphodiesterase/nucleotide pyrophosphatase, with conservation of the catalytic metal ions. Furthermore, many other phosphodiesterases, although not evolutionarily related, have a similar a...

the differential effects of debate and media analysis as relate to enhancing efl learners critical thinking ability and writing performances

critical thinking ability has an important role in education. accordingly, scholars around the world are searching for new ways for teaching and improving students critical thinking ability. in line with the studies in efl contexts supporting the positive relationship between critical thinking and writing performances, this study investigated the differential effects of halverson’s critical thi...

Escherichia coli alkaline phosphatase. Metal binding, protein conformation, and quaternary structure.

Functional Significance of Calcium Binding to Tissue-Nonspecific Alkaline Phosphatase

The conserved active site of alkaline phosphatases (AP) contains catalytically important Zn2+ (M1 and M2) and Mg2+-sites (M3) and a fourth peripheral Ca2+ site (M4) of unknown significance. We have studied Ca2+ binding to M1-4 of tissue-nonspecific AP (TNAP), an enzyme crucial for skeletal mineralization, using recombinant TNAP and a series of M4 mutants. Ca2+ could substitute for Mg2+ at M3, w...