Abstract: A bone targeted alkaline phosphatase comprising a polypeptide having the structure: Z-sALP-Y-spacer-X-Wn-V, wherein sALP is the extracellular domain of the alkaline phosphatase; wherein V is absent or is an amino acid sequence of at least one amino acid; X is absent or is an amino acid sequence of at least one amino acid; Y is absent or is an amino acid sequence of at least one amino acid; Z is absent or is an amino acid sequence of at least one amino acid; and Wn is a polyaspartate or a polyglutamate wherein n=10 to 16. Kits and methods of use thereof.

Abstract: The present invention pertains to the use of the protein phenylalanine ammonia-lyase, as well as the biologically-active derivatives of the said protein for preventing or treating diseases associated with a phenylalanine imbalance in a human or animal body. More particularly, the present invention relates to the therapeutic use of the above-cited molecules for preventing or treating a phenylalanine imbalance in vivo. This invention also deals with therapeutic compositions comprising a pharmaceutically active amount of the above-described therapeutic molecules as well as with therapeutic methods using the said therapeutic compositions. Finally, the present invention relates to processes for selecting more therapeutically-effective variants of said protein as well as to the selected variants themselves.

Abstract: The present invention pertains to the use of the protein phenylalanine ammonia-lyase, as well as the biologically-active derivatives of the said protein for preventing or treating diseases associated with a phenylalanine imbalance in a human or animal body. More particularly, the present invention relates to the therapeutic use of the above-cited molecules for preventing or treating a phenylalanine imbalance in vivo. This invention also deals with therapeutic compositions comprising a pharmaceutically active amount of the above-described therapeutic molecules as well as with therapeutic methods using the said therapeutic compositions. Finally, the present invention relates to processes for selecting more therapeutically-effective variants of said protein as well as to the selected variants themselves.

Abstract: A heparinase derived from Flavobacterium heparinum which meets all requirements for a clinical reagent that can eliminate heparin interference of normal blood function has been developed. The heparinase, derived from Flavobacterium heparinum, is free of a component that inhibits coagulation wherein the anticoagulant component does not bind, and the heparinase does bind, to a polysulfated resin having a pH of 7.0 and a conductivity between 3 and 12 mmhos. It is stable under normal manufacturing, shipping and clinical storage conditions for at least one year. The heparinase in useful in vitro to eliminate the interference in hematological assays due to the presence of heparin. The heparinase is also useful for the in vivo neutralization of heparin during surgical procedures. Advantages of this enzyme are that it achieves neutralization faster and more completely than previously available enzymes and is stable for long periods of time.

Abstract: A heparinase formulation derived from Flavobacterium heparinum which meets all requirements for a clinical reagent that can eliminate heparin interference of normal blood function has been developed. The heparinase, derived from Flavobacterium heparinum, is free of a component that inhibits coagulation. It is stable under normal manufacturing, shipping and clinical storage conditions for at least one year. The heparinase in useful in vitro to eliminate the interference in hematological assays due to the presence of heparin. The heparinase is also useful for the in vivo neutralization of heparin during surgical procedures. Advantages of this preparation are that it achieves neutralization faster and more completely than previously available compositions and is stable for long periods of time.