Linked Life Data

432955

Source:http://linkedlifedata.com/resource/pubmed/id/432955

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1979-6-26
pubmed:abstractText
The mode of tryptophan residue orientation in myosin and action myofilaments of the muscle fiber was studied using polarized ultraviolet (UV) fluorescent microscopy of the muscle fiber was studied using polarized ultraviolet (UV) fluorescent microscopy technique. During an elective extraction of proteine from thick and thin myofillaments changes in UV fluorescence anisotropy of muscle fibers were detected, thus suggesting that tryptophanil residues in myosin may be oriented by their own short axes mostly parallel, but in actin--perpendicular to the muscle fiber axis. The use of acrylamide, an UV fluorescence quencher, is proposed for the control of extraction electivity of proteins from muscle fibers.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0041-3771
pubmed:author
pubmed:issnType
Print
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
171-5
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
[Nature of the orientation of the tryptophan residues in the myosin and actin from striated muscle fiber].
pubmed:publicationType
Journal Article, English Abstract