Linked Life Data

2859

Source:http://linkedlifedata.com/resource/pubmed/id/2859

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1976-4-30
pubmed:abstractText
Influence of pH was studied on the absorption spectra (340-670 nm) and on the curves of abnormal dispersion of optic rotation (220-270 nm) of the lupine ferri-leg-hemoglobin (Lb). pH range of the existence of the lupine Lb native form was determined (pH 5.5-11.0 at 20-25degrees C). It has been shown that not only met-hydroxy transition (which is in a complicated manner connected with the ionization of both ligand-bound water and certain amino acid residues of globin) but the ionization of a group with pK approximately 5, too, in the native molecule produces a heterotropic effect onto the haem. Complex analysis of the acidic and alkaline denaturation evidences that these processes are cooperative and proceed via several stages. pK values and the number of tyrosine residues were determined; it has been shown that these amino acid moieties are "buried" in the protein molecule. The results are discussed on the basis of a tentative model of the lupine Lb spatial suggested by the authors.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0026-8984
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
491-501
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
[Acid-alkaline equilibrium of the ferri-leg-hemoglobin of the lupine (Lupinus luteus L.) Spectral studies].
pubmed:publicationType
Journal Article, English Abstract