FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2329125099> ?p ?o ?g. }

• W2329125099 endingPage "799" @default.
• W2329125099 startingPage "788" @default.
• W2329125099 abstract "The relationship between the assay values of the activities of the stimulatory guanine nucleotide-binding regulatory component (N-protein) of adenylate cyclase by two different methods: reconstitution of plasma membranes of cyc- S49 cells and ADP ribosylation catalyzed by cholera toxin, have not been fully elucidated yet. In the present study, the reconstitution and ADP ribosylation assay methods were utilized, and the relationship between the assay values of the N-protein activities of the erythrocyte membranes from normal subjects and patients with pseudohypoparathyroidism type I (PHP-I) measured by the two methods was investigated. When Lubrol extracts of human erythrocyte membranes were reconstituted with cyc- membranes, the rate of cyclic AMP synthesis reached a constant rate after incubation of 80 minutes at 30 degrees C. This reaction depended on the concentrations of cyc- membranes and Lubrol extracts of the erythrocyte membranes. N-protein activity in the erythrocyte membranes of normal subjects and PHP-I patients assayed by reconstitution of cyc- membranes (mean +/- SD, expressed by % of pooled standard preparation) was 100.1 +/- 13.5 (n = 29) and 82.3 +/- 28.0 (n = 19) respectively. The cholera toxin-catalyzed transfer of [32P]ADP ribose from [32P]NAD to the 42,000-dalton peptide subunit of human erythrocyte N-protein reached a plateau after incubation of 10 minutes at 30 degrees C. This reaction depended on the concentrations of cholera toxin, NAD, and the erythrocyte membranes. N-protein activity in the erythrocyte membranes from normal subjects and PHP-I patients assayed by cholera toxin-catalyzed ADP ribosylation (pmol/mg of protein) was 1.33 +/- 0.20 (n = 7) and 1.15 +/- 0.43 (n = 5) respectively. The correlation between assay values of erythrocyte N-protein activity in PHP-I patients by reconstitution of cyc- membranes (X, % of pooled standard) and cholera toxin-catalyzed ADP ribosylation (Y, % of pooled standard) was recognized as a linear regression: Y = 0.77X + 16.8 (r = 0.981, P less than 0.001). It is thus concluded that the activity of N-protein in human erythrocyte membrane can be assayed by the ADP ribosylation method more simply than by the method of reconstitution of cyc- membranes, with highly close correlation between the values determined by these two methods." @default.
• W2329125099 created "2016-06-24" @default.
• W2329125099 creator A5032481392 @default.
• W2329125099 creator A5033673734 @default.
• W2329125099 creator A5075316546 @default.
• W2329125099 date "1984-01-01" @default.
• W2329125099 modified "2023-10-18" @default.
• W2329125099 title "The Measurement of N-protein Activity in Plasma Membranes : The Comparison of Assay Methods by Reconstitution of cyc<SUP>-</SUP>Membranes and Cholera Toxin-catalyzed ADP Ribosylation" @default.
• W2329125099 cites W1511336559 @default.
• W2329125099 cites W1513226140 @default.
• W2329125099 cites W1603778778 @default.
• W2329125099 cites W182982796 @default.
• W2329125099 cites W1985124610 @default.
• W2329125099 cites W1985185693 @default.
• W2329125099 cites W2029328131 @default.
• W2329125099 cites W2079491912 @default.
• W2329125099 cites W2090114948 @default.
• W2329125099 cites W2100837269 @default.
• W2329125099 cites W2144760024 @default.
• W2329125099 cites W2178536469 @default.
• W2329125099 cites W2341814959 @default.
• W2329125099 cites W2397456260 @default.
• W2329125099 cites W2411570094 @default.
• W2329125099 doi "https://doi.org/10.1507/endocrine1927.60.6_788" @default.
• W2329125099 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/6434354" @default.
• W2329125099 hasPublicationYear "1984" @default.
• W2329125099 type Work @default.
• W2329125099 sameAs 2329125099 @default.
• W2329125099 citedByCount "0" @default.
• W2329125099 crossrefType "journal-article" @default.
• W2329125099 hasAuthorship W2329125099A5032481392 @default.
• W2329125099 hasAuthorship W2329125099A5033673734 @default.
• W2329125099 hasAuthorship W2329125099A5075316546 @default.
• W2329125099 hasBestOaLocation W23291250991 @default.
• W2329125099 hasConcept C134018914 @default.
• W2329125099 hasConcept C153911025 @default.
• W2329125099 hasConcept C180526460 @default.
• W2329125099 hasConcept C181199279 @default.
• W2329125099 hasConcept C185592680 @default.
• W2329125099 hasConcept C25642318 @default.
• W2329125099 hasConcept C2777006276 @default.
• W2329125099 hasConcept C2777367657 @default.
• W2329125099 hasConcept C41625074 @default.
• W2329125099 hasConcept C45510557 @default.
• W2329125099 hasConcept C55493867 @default.
• W2329125099 hasConcept C75520062 @default.
• W2329125099 hasConcept C86803240 @default.
• W2329125099 hasConceptScore W2329125099C134018914 @default.
• W2329125099 hasConceptScore W2329125099C153911025 @default.
• W2329125099 hasConceptScore W2329125099C180526460 @default.
• W2329125099 hasConceptScore W2329125099C181199279 @default.
• W2329125099 hasConceptScore W2329125099C185592680 @default.
• W2329125099 hasConceptScore W2329125099C25642318 @default.
• W2329125099 hasConceptScore W2329125099C2777006276 @default.
• W2329125099 hasConceptScore W2329125099C2777367657 @default.
• W2329125099 hasConceptScore W2329125099C41625074 @default.
• W2329125099 hasConceptScore W2329125099C45510557 @default.
• W2329125099 hasConceptScore W2329125099C55493867 @default.
• W2329125099 hasConceptScore W2329125099C75520062 @default.
• W2329125099 hasConceptScore W2329125099C86803240 @default.
• W2329125099 hasIssue "6" @default.
• W2329125099 hasLocation W23291250991 @default.
• W2329125099 hasLocation W23291250992 @default.
• W2329125099 hasOpenAccess W2329125099 @default.
• W2329125099 hasPrimaryLocation W23291250991 @default.
• W2329125099 hasRelatedWork W1535671912 @default.
• W2329125099 hasRelatedWork W1982975394 @default.
• W2329125099 hasRelatedWork W2019236970 @default.
• W2329125099 hasRelatedWork W2021306367 @default.
• W2329125099 hasRelatedWork W2050556809 @default.
• W2329125099 hasRelatedWork W2052691902 @default.
• W2329125099 hasRelatedWork W2082679991 @default.
• W2329125099 hasRelatedWork W2159918100 @default.
• W2329125099 hasRelatedWork W2286018820 @default.
• W2329125099 hasRelatedWork W2329125099 @default.
• W2329125099 hasVolume "60" @default.
• W2329125099 isParatext "false" @default.
• W2329125099 isRetracted "false" @default.
• W2329125099 magId "2329125099" @default.
• W2329125099 workType "article" @default.