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Article

An active site mutant of human placental alkaline phosphatase with deficient enzymatic activity and preserved immunoreactivity.

Clinica chimica acta; international journal of clinical chemistry - 15 Jan 1990

Narisawa S, Sowadski J M, Millán J L

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Identifiers

PMID: 2178808
DOI: 10.1016/0009-8981(90)90036-r

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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An active site mutant of human placental alkaline phosphatase with deficient enzymatic activity and preserved immunoreactivity.PMID 2178808Read ↗

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Structural evidence of functional divergence in human alkaline phosphatases.Semantic proximity Read ↗

An asparagine at position 417 of tissue-nonspecific alkaline phosphatase is essential for its structure and function as revealed by analysis of the N417S mutation associated with severe hypophosphatasia.Semantic proximity Read ↗

Biology of Human Alkaline Phosphatases with Special Reference to CancerSemantic proximity Read ↗

Mutations of the tissue non-specific alkaline phosphatase gene (TNAP) causing a non-lethal case of perinatal hypophosphatasia.Semantic proximity Read ↗

Retention at the cis-Golgi and delayed degradation of tissue-non-specific alkaline phosphatase with an Asn153-->Asp substitution, a cause of perinatal hypophosphatasia.Semantic proximity Read ↗

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Disulfide bonds are critical for tissue-nonspecific alkaline phosphatase function revealed by analysis of mutant proteins bearing a C(201)-Y or C(489)-S substitution associated with severe hypophosphatasia.Semantic proximity Read ↗

Human Carboxylesterases in Term Placentae: Enzymatic Characterization, Molecular Cloning and Evidence for the Existence of Multiple FormsSemantic proximity Read ↗

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