Linked Life Data

7272325

Source:http://linkedlifedata.com/resource/pubmed/id/7272325

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1981-11-22
pubmed:abstractText
The lactose-blockable lectin activity from fetal calf skeletal muscle has been purified to apparent homogeneity. The purification entails differential centrifugation, ammonium sulfate precipitation, asialofetuin affinity chromatography with a lactose gradient and ion-exchange chromatography on DEAE-cellulose. In the last step, the activity is resolved into a major and minor species, designated ion-exchange-purified lectins I and II, respectively. Both lectin activities are reversibly inhibited by lactose and appear as single bands with identical mobilities on SDS-polyacrylamide gel electrophoresis. Lectin II was not obtained in sufficient quantities for further characterization. Lectin I is characterized by a functional requirement for reducing agents and sensitivity to N-ethylmaleimide, which suggests a role for an essential thiol in its activity. Subunit molecular weight determinations by SDS-polyacrylamide gel electrophoresis (12 000 +/- 1 000) and by gel filtration in 6 M guanidine . HCl (13 000 +/- 1 000), when compared with that obtained under native conditions on Bio-Rad P-60 gels (27 000 +/- 2 000), suggest a true Mr of 25 000 +/- 3 000 for the dimeric molecule. Amino acid composition data, when fitted to this molecular weight, lead to the tentative conclusion that the intact dimer is composed of two very similar but compositionally non-identical chains, designated by alpha and beta. While the only detectable N-terminal amino acid is tryptophan, the isoelectric focusing pattern of lectin I supports this heterodimeric structure. In addition, a lactose-sensitive hemagglutinating activity which can be separated from the lactose-blockade activity by affinity chromatography was also observed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
670
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
110-23
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Physical and chemical characterization of the major lactose-blockable lectin activity from fetal calf skeletal muscle.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't