Richard A. Mulivor

TL;DR: Introduction of this mutation into an otherwise normal cDNA by site-directed mutagenesis abolishes the expression of active enzyme, demonstrating that a defect in the L/B/K ALP gene results in hypophosphatasia and that the enzyme is, therefore, essential for normal skeletal mineralization.

TL;DR: P, like TNSALP, is physiologically active toward PEA, PPi, and PLP in humans, and it is speculated from molecular/crystallographic information, indicating significant similarity of structure of the substrate-binding site of ALPs throughout nature, that all ALP isoenzymes recognize these same three phosphocompound substrates.

TL;DR: Inhibition studies have been carried out on a series of ALPs derived from liver, bone, kidney, placenta and intestine, using L‐phenylalanine, L‐homoarginine,L‐leucine and L‐leucyl‐ glyoyl‐glycine as inhibitors.

TL;DR: A survey of intestinal samples from fetuses and premature infants of various gestational ages indicated that the changeover from the synthesis of fetal to adult intestinal enzyme begins at about 28-32 weeks of gestation.

TL;DR: The combined use of ultrasonography, analysis of amniotic fluid alpha-fetoprotein, and the measurement of the bone/liver ALP in cultured amniotics fluid cells would appear to be the best approach to the prenatal diagnosis of the severe, early onset form of hypophosphatasia.