Matches in SemOpenAlex for { <https://semopenalex.org/work/W2042296927> ?p ?o ?g. }
Showing items 1 to 70 of
70
with 100 items per page.
- W2042296927 endingPage "324" @default.
- W2042296927 startingPage "320" @default.
- W2042296927 abstract "Tay-Sachs disease (TSD) is a neurodegenerative genetic disorder caused by a deficiency of beta-hexosaminidase A (Hex A) activity. To diagnose TSD and to screen for TSD heterozygosity, laboratories use an assay that exploits the differential thermolability of the major beta-hexosaminidase isoenzymes, Hex A and Hex B. At 50–52°C Hex A is labile, and Hex B is stable. We previously noted that the stability of leukocyte Hex B at 52°C varied significantly, depending on the sample concentration in the incubation mixture. We have now examined this phenomenon in enzyme from cultured cells used for prenatal and postnatal diagnostic testing. We found that fibroblast Hex A and Hex B behave similarly to the leukocyte isoenzymes. In control and TSD fibroblasts there was a linear correlation between Hex B thermostability and sample concentration; at lower sample concentrations Hex B was less stable than at higher concentrations. Dialysis of the samples prior to heat treatment did not change the thermostability properties of Hex B, indicating that the change in stability is not due to a soluble low molecular weight substance. Cultured amniotic fluid cell and chorionic villus cell Hex B had a similar, but less pronounced, instability at low sample concentrations. Therefore, the unusual thermolability properties of Hex B, first detected for leukocyte Hex B, were noted in multiple tissues. Based on these data, we suggest that the concentration of cell extract be stringently controlled when the heat-inactivation method is used for the pre- or postnatal diagnosis of TSD, and that supplementation with non-thermolability-based beta-hexosaminidase assays should be employed as needed. © 1996 Wiley-Liss, Inc." @default.
- W2042296927 created "2016-06-24" @default.
- W2042296927 creator A5081611869 @default.
- W2042296927 creator A5083022460 @default.
- W2042296927 creator A5084022283 @default.
- W2042296927 date "1996-11-11" @default.
- W2042296927 modified "2023-09-26" @default.
- W2042296927 title "Unusual thermolability properties of beta-hexosaminidase: Studies of enzyme from cultured cells and clinical implications" @default.
- W2042296927 cites W1157912633 @default.
- W2042296927 cites W1515758336 @default.
- W2042296927 cites W1566325294 @default.
- W2042296927 cites W1775749144 @default.
- W2042296927 cites W2006746571 @default.
- W2042296927 cites W2024036407 @default.
- W2042296927 cites W2172877688 @default.
- W2042296927 cites W4301110865 @default.
- W2042296927 doi "https://doi.org/10.1002/(sici)1096-8628(19961111)65:4<320::aid-ajmg14>3.0.co;2-w" @default.
- W2042296927 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8923943" @default.
- W2042296927 hasPublicationYear "1996" @default.
- W2042296927 type Work @default.
- W2042296927 sameAs 2042296927 @default.
- W2042296927 citedByCount "3" @default.
- W2042296927 crossrefType "journal-article" @default.
- W2042296927 hasAuthorship W2042296927A5081611869 @default.
- W2042296927 hasAuthorship W2042296927A5083022460 @default.
- W2042296927 hasAuthorship W2042296927A5084022283 @default.
- W2042296927 hasConcept C119795356 @default.
- W2042296927 hasConcept C126322002 @default.
- W2042296927 hasConcept C134018914 @default.
- W2042296927 hasConcept C153911025 @default.
- W2042296927 hasConcept C181199279 @default.
- W2042296927 hasConcept C185592680 @default.
- W2042296927 hasConcept C25642318 @default.
- W2042296927 hasConcept C2781216036 @default.
- W2042296927 hasConcept C55493867 @default.
- W2042296927 hasConcept C71924100 @default.
- W2042296927 hasConcept C86803240 @default.
- W2042296927 hasConceptScore W2042296927C119795356 @default.
- W2042296927 hasConceptScore W2042296927C126322002 @default.
- W2042296927 hasConceptScore W2042296927C134018914 @default.
- W2042296927 hasConceptScore W2042296927C153911025 @default.
- W2042296927 hasConceptScore W2042296927C181199279 @default.
- W2042296927 hasConceptScore W2042296927C185592680 @default.
- W2042296927 hasConceptScore W2042296927C25642318 @default.
- W2042296927 hasConceptScore W2042296927C2781216036 @default.
- W2042296927 hasConceptScore W2042296927C55493867 @default.
- W2042296927 hasConceptScore W2042296927C71924100 @default.
- W2042296927 hasConceptScore W2042296927C86803240 @default.
- W2042296927 hasIssue "4" @default.
- W2042296927 hasLocation W20422969271 @default.
- W2042296927 hasLocation W20422969272 @default.
- W2042296927 hasOpenAccess W2042296927 @default.
- W2042296927 hasPrimaryLocation W20422969271 @default.
- W2042296927 hasRelatedWork W1966695668 @default.
- W2042296927 hasRelatedWork W2008272687 @default.
- W2042296927 hasRelatedWork W2012680209 @default.
- W2042296927 hasRelatedWork W2037200938 @default.
- W2042296927 hasRelatedWork W2048574507 @default.
- W2042296927 hasRelatedWork W2069489889 @default.
- W2042296927 hasRelatedWork W2071237287 @default.
- W2042296927 hasRelatedWork W2108221712 @default.
- W2042296927 hasRelatedWork W2110054463 @default.
- W2042296927 hasRelatedWork W2067403872 @default.
- W2042296927 hasVolume "65" @default.
- W2042296927 isParatext "false" @default.
- W2042296927 isRetracted "false" @default.
- W2042296927 magId "2042296927" @default.
- W2042296927 workType "article" @default.