Topic
Esterase D
About: Esterase D is a research topic. Over the lifetime, 234 publications have been published within this topic receiving 4405 citations.
Papers published on a yearly basis
Papers
TL;DR: The present paper describes yet a further human red cell esterase, which is different from the red cell A, B aiid C esterases, the carbonic anhydrase isozymes, and from acetylcholinesterase in their structure and function.
Abstract: Tashian (1 961, 1969) demonstrated several different esterases in human red cells by electrophoresis. Azo dye coupling techniques were used to locate the esterase isozymes. Three main groups of esterases were defined on the basis of their electrophoretic properties, substrate specificities and inhibition characteristics, and were referred to as the A, B and C esterases. Isozymes of carbonic anhydrase, which also has esteratic activity, were also demonstrated using essentially similar techniques. Fig. 1, which is based on Tashian's work, shows a diagrammatic representation of the various red cell esterase isozymes after electrophoresis of haemolysates in borate starch gels at pH 8.0-8-6. The A esterases are subdivided into three sets of isozymes, A,, A, and As, which differ electrophoretically and in their storage properties and inhibition characteristics ; also the As isozymes have a larger molecular size than A, or A,. Inherited variants of these isozymes are rare in man but two different variant phenotypes have been reported (Tashian & Shaw, 1962; Tashian, 1965). They are of particular interest because each of the three subgroups of A esterase are affected in the variant isozyme patterns suggesting that A,, A, and As contain a common subunit. Family studies on one of the variants indicated that this esterase A locus is autosomal. Esterase B is primarily a butyryl esterase and no variants have been reported in population surveys to date. Esterase C is a rather weakly staining invariate acetyl esterase. Several different variants of the carbonic anhydrase isozyme CA I (or B) have been recorded in the literature (see Tashian, 1969) but they are all individually rare except in certain cases where they have been identified in small isolated populations, e.g. the CA I, variant in Guam and Saipan. The CA 1 locus is autosomal and the variants do not affect CA I1 (or C). The latter is determined at a separate autosomal locus and recent studies (Moore, Funakoshi & Deutsch, 1971) using an immunological detection technique have led to the recognition of a genetic polymorphism of CA 11 in Blacks. Another esterase which occurs in red cells is acetylcholinesterase. This is membrane bound and not therefore readily detected by electrophoresis of simple lysates. The present paper describes yet a further human red cell esterase. It will be referred to as esterase D (Es D). It was discovered by the use of the fluorogenic substrates, 4-methyl-umbelliferyl acetate and 4-methyl-umbelliferyl butyrate, for the detection of esterase isozymes after starch gel electrophoresis. The isozymes of this new esterase are different from the red cell A, B aiid C esterases, the carbonic anhydrase isozymes, and from acetylcholinesterase in their
401 citations
TL;DR: The discovery of a polymorphic marker genetically linked to the WD locus has profound implications both for investigation of the primary gene defect and for clinical services.
Abstract: Wilson disease (WD) is an autosomal recessively inherited disorder of copper metabolism for which the basic defect is still unknown. Twenty-seven autosomal markers were investigated for linkage in a large inbred kindred with affected individuals in two generations. Also, serum copper and ceruloplasmin were measured on all available members. Close linkage (theta = 0.06) with a logarithm of odds (lod) score of 3.21 was found between the gene for WD and the esterase D locus. Efficient detection of linkage was made possible by the use of a multisibship inbred pedigree. The discovery of a polymorphic marker genetically linked to the WD locus has profound implications both for investigation of the primary gene defect and for clinical services.
286 citations
TL;DR: The data presented suggest that the gene for the human enzyme MOR-M can be assigned to chromosome 7, whilst those for MPI and PK-3 are on chromosome 15.
Abstract: Eleven independent man-mouse hybrids and 40 subclones from four to them were analysed for up to 42 enzyme markers. Nine subclones from three hybrid lines were fully karyotyped. The data presented suggest that the gene for the human enzyme MOR-M can be assigned to chromosome 7, whilst those for MPI and PK-3 are on chromosome 15. The use of a small number of well-characterized hybrids for gene assigments is discussed as well as the significance of some known human linkage relationships.
165 citations
TL;DR: Downstream of flhA, the Paracoccus denitrificans gene encoding glutathione-dependent formaldehyde dehydrogenase, an open reading frame was identified and called fghA, and a mutant was unable to grow on methanol and methylamine, indicating that the enzyme is essential for methylotrophic growth.
Abstract: Downstream of flhA, the Paracoccus denitrificans gene encoding glutathione-dependent formaldehyde dehydrogenase, an open reading frame was identified and called fghA. The gene product of fghA showed appreciable similarity with human esterase D and with the deduced amino acid sequences of open reading frames found in Escherichia coli, Haemophilus influenzae, and Saccharomyces cerevisiae. Mutating fghA strongly reduced S-formylglutathione hydrolase activity. The mutant was unable to grow on methanol and methylamine, indicating that the enzyme is essential for methylotrophic growth. S-Formylglutathione hydrolase appears to be part of a formaldehyde detoxification pathway that is universal in nature.
121 citations
TL;DR: No electrophoretic variants were identified in a limited population survey of post-mortem tissues from adults and foetuses, except for the previously described esterase D (ESD) phenotypes.
Abstract: 1. The esterase isozymes of human tissues have been investigated using the technique of starch-gel electrophoresis. Conventional naphthyl-azo dye linked stains and new fluorogenic staining methods were used to detect the isozymes. 2. Multiple isozymes were identified in every tissue and they were characterized in terms of their electrophoretic mobility, tissue distribution, developmental changes in utero, substrate specificity, inhibition properties and molecular weight. On these criteria 13 sets of esterase isozymes were identified, in addition to the esterase isozymes due to cholinesterase and carbonic anhydrase. 3. The data suggest that the 13 sets of isozymes are determined by at least nine different structural gene loci. 4. No electrophoretic variants were identified in a limited population survey of post-mortem tissues from adults and foetuses, except for the previously described esterase D (ESD) phenotypes.
111 citations
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| Year | Papers |
|---|---|
| 2017 | 1 |
| 2013 | 1 |
| 2012 | 1 |
| 2011 | 1 |
| 2010 | 1 |
| 2009 | 3 |