Linked Life Data

3558696

Source:http://linkedlifedata.com/resource/pubmed/id/3558696

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1987-5-13
pubmed:abstractText
The sugar-chain heterogeneity of alkaline phosphatases (ALPs) from various human organs was investigated by using the serial lectin affinity technique. This technique revealed a possible structure of the sugar chain(s) of ALP isozymes and clarified a difference in affinity on the lectin column not only among three genetically different isozymes (liver/bone/kidney, intestinal and placental types) but also among liver, bone, and kidney ALPs. Lectin-binding profiles of ALPs in these human organs closely resembled those in the corresponding organs of the rat, as reported previously, suggesting that heterogeneities in sugar chains of ALPs have a specificity for the respective organs rather than being species-specific. Lectin-binding profiles of tumour-produced placental and liver ALPs were significantly different from those of ALPs in the respective normal organs. However, the two altered ALPs exhibited similar lectin-binding affinities. Isoelectric focusing analysis showed essentially no difference in protein charge between the normal and tumor-produced ALPs. Moreover, tumour-produced ALPs had the same N-terminal amino acid sequence and peptide mapping as normal ALPs. From these results, it is possible to suggest that organ-specific sugar chains in ALP isozymes are changed into those peculiar to tumours in association with malignant transformation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9673
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
413
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
65-78
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Sugar-chain heterogeneity of human alkaline phosphatases: differences between normal and tumour-associated isozymes.
pubmed:publicationType
Journal Article, Comparative Study