Linked Life Data

9612569

Source:http://linkedlifedata.com/resource/pubmed/id/9612569

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1998-8-13
pubmed:abstractText
The formation of biologically active hemoglobin fragments in human erythrocytes was studied. The structures of 33 peptide products of intraerythrocytic hemoglobin cleavage were determined. Based on an analysis of these sequences, a model of the stepwise degradation of the hemoglobin alpha- and beta-chains was suggested. The processes of peptide formation in a cell-free erythrocyte lysate system were studied. The involvement of an enzymatic complex of the cell membrane fraction was demonstrated. It was found that the cells of a surviving human erythrocyte culture secrete short (of 5-20 amino acid residues) peptides, and the structures of 36 peptides were determined. The dynamics of peptide secretion was investigated, and preliminary data on the energy-dependence of this process were obtained. Based on the experimental results, a model describing erythrocytes as an endocrine gland was suggested.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0132-3423
pubmed:author
pubmed:issnType
Print
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
271-81
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
[Proteolytic degradation of hemoglobin in erythrocytes results in formation of biologically active peptides].
pubmed:affiliation
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
pubmed:publicationType
Journal Article, English Abstract