Linked Life Data

97516

Source:http://linkedlifedata.com/resource/pubmed/id/97516

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1978-9-30
pubmed:abstractText
A sarcoplasmic calcium-binding protein (SCP) has been purified from the muscle of the protochordate Amphioxus and shown to be more similar to invertebrate SCP's than to their counterpart found in vertebrates, i.e. parvalbumins. The Amphioxus protein has a pI of 4.9, is rich in tyrosine and tryptophan, has a molecular weight of 22,000 and binds strongly 2Ca2+ with a pK of 7.88. Magnesium competes with calcium for only one of the two metal-binding sites and induces positive cooperativity in Ca2+ binding. In cyclostome muscle (lamprey and hagfish), no protein with high affinity for Ca2+ or Mg2+ could be found, irrespective of molecular weight. Instead, a protein with moderate affinity for Ca2+ (less than or equal to 10(5) M(-1)) was detected: it has a molecular weight of 60,000 and might be quite ubiquitous, as the presence of a similar protein has been reported both in red and white muscle of vertebrates such as chicken and rabbit.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0300-8177
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
85-93
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
Sarcoplasmic calcium-binding proteins in protochordate and cyclostome muscle: characterization of a new protein from amphioxus.
pubmed:publicationType
Journal Article