Linked Life Data

6746585

Source:http://linkedlifedata.com/resource/pubmed/id/6746585

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1984-8-27
pubmed:abstractText
Bovine band 3 in membrane-bound and solubilized states was digested with chymotrypsin, trypsin, and papain. Bovine band 3 in red blood cells was fragmented by the proteases in a 5 mM NaH2PO4-Na2HPO4 buffer containing 0.3 M glucose, pH 8.0, but not in a 5 mM NaH2PO4-Na2HPO4 buffer containing 0.15 M NaCl, pH 8.0, in which human band 3 is cleaved by chymotrypsin and papain. When compared with the known data for human band 3, however, major fragments of bovine band 3 derived from intact cells, inside-out vesicles and unsealed ghosts were similar to those of human band 3, except that tryptic fragments were formed on the extracellular attack. The results suggest that bovine band 3 adopts a quite similar molecular arrangement in the membrane to in the human case. However, it was strongly suggested by molecular weight evaluation of fragments that the only detectable water-soluble 38,000-39,000 dalton fragment does not account for the entire hydrophilic pole of the band 3 molecule exposed in the cytoplasmic region of the membrane. When isolated band 3 was treated with the enzymes in a 2% solution of nonaethyleneglycol n-dodecyl ether, the major product was indistinguishable on sodium dodecyl sulfate-gel from the water-soluble fragment of the cytoplasmic domain origin of band 3. This fragment lost its resistance to further enzymatic degradation when treated with dimethylmaleic anhydride, thus band 3 oligomers were converted into their monomers. The chymotryptic 38,000 dalton water-soluble fragment obtained in nonaethyleneglycol n-dodecyl ether solution was a subfragment of a 50,000 dalton piece which was produced in a 2% solution of deoxycholate after chymotrypsin treatment of band 3.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
95
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1019-29
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Proteolytic digestion of band 3 from bovine erythrocyte membranes in membrane-bound and solubilized states.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't