Matches in SemOpenAlex for { <https://semopenalex.org/work/W4243444927> ?p ?o ?g. }
Showing items 1 to 81 of
81
with 100 items per page.
- W4243444927 endingPage "1189" @default.
- W4243444927 startingPage "1182" @default.
- W4243444927 abstract "In hereditary pyropoikilocytosis (HPP), the red cell membrane skeletons exhibit a mechanical instability that can be correlated to defective self-association of spectrin heterodimers. To determine the underlying molecular defect, we have subjected HPP spectrin to limited tryptic digestion, followed by one- and two-dimensional separations of the peptides. Two of the HPP kindreds exhibited a marked decrease in 80,000- dalton peptide (previously identified as the spectrin dimer-dimer contact domain of the alpha-subunit) and a concomitant increase of the 74,000-dalton polypeptide (presumably derived from the 80,000-dalton domain) and a decrease in a 22,000-dalton polypeptide. We now report tryptic digests of two other HPP kindred that are characterized by a decrease or complete absence of the 80,000-dalton tryptic fragment, with a concomitant increase in fragments at 46,000 and 17,000 daltons. The 46,000-dalton fragment separated into multiple spots on isoelectric focusing, ranging in isoelectric point from 5.25 to 5.35, and the 17,000-dalton fragment focused to a single spot at 5.4. Minor fragments at 56,000 and 22,000 daltons were also decreased, while a 38,000-dalton fragment increased. Limited tryptic digestion of the separated alpha- and beta-subunits revealed that the 74,000-dalton fragment in the first group of patients and the 46,000-dalton fragment in the second group of patients were derived from the alpha-subunit. Both subtypes exhibited a similar defect of spectrin self-association, with 30%-38% of spectrin dimers in O degrees C extracts. The results indicate that at least two distinct forms of structurally defective spectrin may give rise to the clinical presentation of HPP." @default.
- W4243444927 created "2022-05-12" @default.
- W4243444927 creator A5016395763 @default.
- W4243444927 creator A5047148281 @default.
- W4243444927 creator A5048022683 @default.
- W4243444927 creator A5052131838 @default.
- W4243444927 creator A5086351363 @default.
- W4243444927 date "1983-12-01" @default.
- W4243444927 modified "2023-09-27" @default.
- W4243444927 title "Molecular heterogeneity of hereditary pyropoikilocytosis: identification of a second variant of the spectrin alpha-subunit" @default.
- W4243444927 doi "https://doi.org/10.1182/blood.v62.6.1182.bloodjournal6261182" @default.
- W4243444927 hasPublicationYear "1983" @default.
- W4243444927 type Work @default.
- W4243444927 citedByCount "0" @default.
- W4243444927 crossrefType "journal-article" @default.
- W4243444927 hasAuthorship W4243444927A5016395763 @default.
- W4243444927 hasAuthorship W4243444927A5047148281 @default.
- W4243444927 hasAuthorship W4243444927A5048022683 @default.
- W4243444927 hasAuthorship W4243444927A5052131838 @default.
- W4243444927 hasAuthorship W4243444927A5086351363 @default.
- W4243444927 hasBestOaLocation W42434449271 @default.
- W4243444927 hasConcept C104292427 @default.
- W4243444927 hasConcept C104317684 @default.
- W4243444927 hasConcept C142669718 @default.
- W4243444927 hasConcept C1491633281 @default.
- W4243444927 hasConcept C153911025 @default.
- W4243444927 hasConcept C159110408 @default.
- W4243444927 hasConcept C178790620 @default.
- W4243444927 hasConcept C181199279 @default.
- W4243444927 hasConcept C185592680 @default.
- W4243444927 hasConcept C2775944032 @default.
- W4243444927 hasConcept C2779546866 @default.
- W4243444927 hasConcept C49453240 @default.
- W4243444927 hasConcept C50244902 @default.
- W4243444927 hasConcept C50476208 @default.
- W4243444927 hasConcept C55493867 @default.
- W4243444927 hasConcept C64943373 @default.
- W4243444927 hasConcept C71924100 @default.
- W4243444927 hasConcept C83730767 @default.
- W4243444927 hasConcept C86803240 @default.
- W4243444927 hasConcept C96294017 @default.
- W4243444927 hasConceptScore W4243444927C104292427 @default.
- W4243444927 hasConceptScore W4243444927C104317684 @default.
- W4243444927 hasConceptScore W4243444927C142669718 @default.
- W4243444927 hasConceptScore W4243444927C1491633281 @default.
- W4243444927 hasConceptScore W4243444927C153911025 @default.
- W4243444927 hasConceptScore W4243444927C159110408 @default.
- W4243444927 hasConceptScore W4243444927C178790620 @default.
- W4243444927 hasConceptScore W4243444927C181199279 @default.
- W4243444927 hasConceptScore W4243444927C185592680 @default.
- W4243444927 hasConceptScore W4243444927C2775944032 @default.
- W4243444927 hasConceptScore W4243444927C2779546866 @default.
- W4243444927 hasConceptScore W4243444927C49453240 @default.
- W4243444927 hasConceptScore W4243444927C50244902 @default.
- W4243444927 hasConceptScore W4243444927C50476208 @default.
- W4243444927 hasConceptScore W4243444927C55493867 @default.
- W4243444927 hasConceptScore W4243444927C64943373 @default.
- W4243444927 hasConceptScore W4243444927C71924100 @default.
- W4243444927 hasConceptScore W4243444927C83730767 @default.
- W4243444927 hasConceptScore W4243444927C86803240 @default.
- W4243444927 hasConceptScore W4243444927C96294017 @default.
- W4243444927 hasIssue "6" @default.
- W4243444927 hasLocation W42434449271 @default.
- W4243444927 hasOpenAccess W4243444927 @default.
- W4243444927 hasPrimaryLocation W42434449271 @default.
- W4243444927 hasRelatedWork W17138194 @default.
- W4243444927 hasRelatedWork W23670794 @default.
- W4243444927 hasRelatedWork W27237450 @default.
- W4243444927 hasRelatedWork W3289316 @default.
- W4243444927 hasRelatedWork W34567185 @default.
- W4243444927 hasRelatedWork W34813706 @default.
- W4243444927 hasRelatedWork W38636490 @default.
- W4243444927 hasRelatedWork W39185923 @default.
- W4243444927 hasRelatedWork W39510538 @default.
- W4243444927 hasRelatedWork W7175571 @default.
- W4243444927 hasVolume "62" @default.
- W4243444927 isParatext "false" @default.
- W4243444927 isRetracted "false" @default.
- W4243444927 workType "article" @default.