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hypophosphatasia/carbohydrate
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Enhancement of drug delivery to bone: characterization of human tissue-nonspecific alkaline phosphatase tagged with an acidic oligopeptide.
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Hypophosphatasia is caused by deficiency of activity of the tissue-nonspecific alkaline phosphatase (TNSALP), resulting in a defect of bone mineralization. Enzyme replacement therapy (ERT) with partially purified plasma enzyme was attempted but with little clinical improvement. Attaining clinical
[The metabolic basis of generalized skeletal dysplasia (author's transl)].
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Numerous control systems are involved in the growth and differentiation of chondro-osseous tissue. Theoretically, the failure of each single step will result in a peculiar skeletal dysplasia. The resulting disorders are caused by errors in the metabolism of collagen, minerals, complex carbohydrates
Glycosylation differences contribute to distinct catalytic properties among bone alkaline phosphatase isoforms.
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Three circulating human bone alkaline phosphatase (BALP) isoforms (B1, B2, and B/I) can be distinguished in healthy individuals and a fourth isoform (B1x) has been discovered in patients with chronic kidney disease and in bone tissue. The present study was designed to correlate differing
The human alkaline phosphatases: what we know and what we don't know.
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A review of the human alkaline phosphatases dealing specifically with (1) the gene loci, (2) characterization and discrimination of the various enzymes, (3) polymorphism at the enzyme level, (4) cDNA and gene structures, (5) membrane binding, (6) the carbohydrate moieties, (7) hypophosphatasia, (8)
Disorders affecting vitamin B6 metabolism.
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Vitamin B6 is present in our diet in many forms, however, only pyridoxal 5'-phosphate (PLP) can function as a cofactor for enzymes. The intestine absorbs nonphosphorylated B6 vitamers, which are converted by specific enzymes to the active PLP form. The role of PLP is enabled by
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