Matches in SemOpenAlex for { <https://semopenalex.org/work/W2355328384> ?p ?o ?g. }
Showing items 1 to 83 of
83
with 100 items per page.
- W2355328384 endingPage "415" @default.
- W2355328384 startingPage "411" @default.
- W2355328384 abstract "The glycosylation of platelets may prolong their life-span when being transfused after preservation under 4 degrees C, therefore this study was aimed to investigate the effect of glycosylation on morphology, ultrastructure, function and membrane glycoprotein of platelets. The experiments were divided into 3 groups: group preserved in room temperature (RT group), group preserved in 4 degrees C (4T group) and group UDP-Gal glycosylated and preserved in 4 degrees C (U+4T group). The binding rate of RCA I lectin and expression of platelet surface markers CD62P, CD42b were determined by flow cytometry. Morphology and ultrastructure of platelets were observed by light microscopy, scanning electron microscopy (SEM) and transmission electron microscopy (TEM). Platelets aggregation was detected by aggregometer. The results showed that the binding rate of RCAI in U+4T group significantly higher than that in RT group (p<0.01), no obvious changes was found in ultrastructure of glycosylated platelets, as compared with fresh platelets. Some morphologic changes, such as pseudopodium could be observed in 4T group. The aggregation rate of platelets in U+4T group reached to 50% of RT group. The expression levels of CD42b and CD62P, and the binding rate of annexin V in U+4T group were not significantly different from that in RT group. It is concluded that UDP-Gal can effectively cause galactosylation of platelets, and the platelets modified with UDP-Gal remain normal morphology, ultrastructure and function." @default.
- W2355328384 created "2016-06-24" @default.
- W2355328384 creator A5013415765 @default.
- W2355328384 creator A5014867897 @default.
- W2355328384 creator A5056835620 @default.
- W2355328384 creator A5079347787 @default.
- W2355328384 creator A5084341192 @default.
- W2355328384 date "2008-04-01" @default.
- W2355328384 modified "2023-09-27" @default.
- W2355328384 title "[Morphology, ultrastructure and function of glycosylation-modified chilled blood platelets]." @default.
- W2355328384 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18426676" @default.
- W2355328384 hasPublicationYear "2008" @default.
- W2355328384 type Work @default.
- W2355328384 sameAs 2355328384 @default.
- W2355328384 citedByCount "0" @default.
- W2355328384 crossrefType "journal-article" @default.
- W2355328384 hasAuthorship W2355328384A5013415765 @default.
- W2355328384 hasAuthorship W2355328384A5014867897 @default.
- W2355328384 hasAuthorship W2355328384A5056835620 @default.
- W2355328384 hasAuthorship W2355328384A5079347787 @default.
- W2355328384 hasAuthorship W2355328384A5084341192 @default.
- W2355328384 hasConcept C105702510 @default.
- W2355328384 hasConcept C153911025 @default.
- W2355328384 hasConcept C185592680 @default.
- W2355328384 hasConcept C203014093 @default.
- W2355328384 hasConcept C26828662 @default.
- W2355328384 hasConcept C2777313579 @default.
- W2355328384 hasConcept C499950583 @default.
- W2355328384 hasConcept C54355233 @default.
- W2355328384 hasConcept C553184892 @default.
- W2355328384 hasConcept C55493867 @default.
- W2355328384 hasConcept C86803240 @default.
- W2355328384 hasConcept C87555872 @default.
- W2355328384 hasConcept C88634738 @default.
- W2355328384 hasConcept C89560881 @default.
- W2355328384 hasConcept C95444343 @default.
- W2355328384 hasConceptScore W2355328384C105702510 @default.
- W2355328384 hasConceptScore W2355328384C153911025 @default.
- W2355328384 hasConceptScore W2355328384C185592680 @default.
- W2355328384 hasConceptScore W2355328384C203014093 @default.
- W2355328384 hasConceptScore W2355328384C26828662 @default.
- W2355328384 hasConceptScore W2355328384C2777313579 @default.
- W2355328384 hasConceptScore W2355328384C499950583 @default.
- W2355328384 hasConceptScore W2355328384C54355233 @default.
- W2355328384 hasConceptScore W2355328384C553184892 @default.
- W2355328384 hasConceptScore W2355328384C55493867 @default.
- W2355328384 hasConceptScore W2355328384C86803240 @default.
- W2355328384 hasConceptScore W2355328384C87555872 @default.
- W2355328384 hasConceptScore W2355328384C88634738 @default.
- W2355328384 hasConceptScore W2355328384C89560881 @default.
- W2355328384 hasConceptScore W2355328384C95444343 @default.
- W2355328384 hasIssue "2" @default.
- W2355328384 hasLocation W23553283841 @default.
- W2355328384 hasLocation W23553283842 @default.
- W2355328384 hasOpenAccess W2355328384 @default.
- W2355328384 hasPrimaryLocation W23553283841 @default.
- W2355328384 hasRelatedWork W1986899767 @default.
- W2355328384 hasRelatedWork W2025634312 @default.
- W2355328384 hasRelatedWork W2036342545 @default.
- W2355328384 hasRelatedWork W2058121024 @default.
- W2355328384 hasRelatedWork W2064376293 @default.
- W2355328384 hasRelatedWork W2079600768 @default.
- W2355328384 hasRelatedWork W2102880973 @default.
- W2355328384 hasRelatedWork W2254545890 @default.
- W2355328384 hasRelatedWork W2290535702 @default.
- W2355328384 hasRelatedWork W2342298633 @default.
- W2355328384 hasRelatedWork W2401573014 @default.
- W2355328384 hasRelatedWork W2405752695 @default.
- W2355328384 hasRelatedWork W2409357176 @default.
- W2355328384 hasRelatedWork W2415557702 @default.
- W2355328384 hasRelatedWork W2468472454 @default.
- W2355328384 hasRelatedWork W2471134422 @default.
- W2355328384 hasRelatedWork W2571438776 @default.
- W2355328384 hasRelatedWork W2577523996 @default.
- W2355328384 hasRelatedWork W2742928906 @default.
- W2355328384 hasRelatedWork W2980943496 @default.
- W2355328384 hasVolume "16" @default.
- W2355328384 isParatext "false" @default.
- W2355328384 isRetracted "false" @default.
- W2355328384 magId "2355328384" @default.
- W2355328384 workType "article" @default.