Linked Life Data

451

Source:http://linkedlifedata.com/resource/pubmed/id/451

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1976-2-20
pubmed:abstractText
Comparative studies of protein structure and function can be quite interesting by themselves, and even more interesting when interpreted with respect to an animal's physiology. In the case of fish hemoglobins, some success in the latter has been achieved but there are still many unsolved problems. It appears that comparative physiology and biochemistry have entered an era where results from comparative studies can shed a great deal of light on biochemical mechanisms in general. The trout hemoglobin system is an example. Distinctive hemoglobins in this system are presently being used as high resolution probes of the ligand-binding mechanism. Characterization of the multiple, structurally distinct subunits of the 60S Limulus hemocyanin molecule may similarly aid in understanding its function. Our studies suggest the possibility of using Limulus hemocyanin and other hemocyanins as structural homologs and analogs of more complex macromolecular arrays. The rapid development of molecular structural data from X-ray crystallographers combined with the vast data of comparative physiology and biochemistry makes this one of the most exciting areas in present day science.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0022-104X
pubmed:author
pubmed:issnType
Print
pubmed:volume
194
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
155-74
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
Hemoglobins and hemocyanins: comparative aspects of structure and function.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Review