Linked Life Data

3017764

Source:http://linkedlifedata.com/resource/pubmed/id/3017764

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1986-10-23
pubmed:databankReference
pubmed:abstractText
The complete amino acid sequence of the large subunit (catalytic subunit) of human low-Ca2+-requiring-calcium-activated neutral protease (muCANP) was deduced from its cDNA base sequence. It is composed of 714 amino acid residues and its sequence is highly homologous to the chicken CANP sequence determined previously. Human muCANP, like chicken CANP, has a clear 4-domain structure, and their fundamental structures are essentially the same, although their Ca2+ sensitivities are significantly different. The role of each domain in the Ca2+ sensitivity and protease activity of CANP is discussed on the basis of sequence comparison.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
205
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
313-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Complete amino acid sequence of the large subunit of the low-Ca2+-requiring form of human Ca2+-activated neutral protease (muCANP) deduced from its cDNA sequence.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't