Further characterization of the human fumarase variant, FH2–1
- 1 October 1979
- journal article
- Published by Wiley in Annals of Human Genetics
- Vol. 43 (2) , 103-108
- https://doi.org/10.1111/j.1469-1809.1979.tb02002.x
Abstract
1. Further investigation of fumarase using lymphoblastoid cells derived from an individual of the FH 2--1 phenotype has confirmed that the mitochondrial (FHM) and soluble (FHS) forms of fumarase are determined at the same structural locus. 2. The FH 2--1 variant is associated with enzyme deficiency: c. 70% of normal in lymphoblastoid cells and c. 20% of normal in red cells. 3. The pH optimum and apparent Michaelis constant of the variant fumarase were normal but heat-inactivation studies suggest that the isozymes containing polypeptides determined by the variant allele are unstable.Keywords
This publication has 4 references indexed in Scilit:
- The genetic determination of fumarase isozymes in human tissuesAnnals of Human Genetics, 1979
- International Committee for Standardization in Haematology: Recommended Methods for Red‐Cell Enzyme Analysis*British Journal of Haematology, 1977
- Presence of two forms of fumarase (fumarate hydratase E.C. 4.2.1.2) in mammalian cells: Immunological characterization and genetic analysis in somatic cell hybrids. Confirmation of the assignment of a gene necessary for the enzyme expression to human chromosome 1Biochemical Genetics, 1975
- Studies of the Enzyme Fumarase. II.1 Isolation and Physical Properties of Crystalline EnzymeJournal of the American Chemical Society, 1954